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Description:

Ciliary Neurotrophic Factor Receptor Human Recombinant

Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.

Product # :

CYT-883

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Description

CNTFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (23-342 a.a) and having a molecular mass of 38.1kDa. CNTFR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNTFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
Synonyms
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.
Background
Unveiling the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Insights and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) holds a crucial role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper discusses the significance of Human Recombinant CNTFR, its production methods, and its potential applications in neurobiology and therapeutic interventions. The review sheds light on the pivotal role of CNTFR in neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, plays a pivotal role in transmitting CNTF-mediated signals to the cell. The availability of Human Recombinant CNTFR allows researchers to investigate its role in neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's involvement in modulating neuronal health and promoting regeneration makes it an essential component in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and initiate downstream signaling pathways. Activation of intracellular signaling cascades, such as JAK/STAT and MAPK, contributes to the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is produced through gene expression in suitable host cells, often employing bacterial or mammalian systems. Ensuring proper folding and post-translational modifications is essential to maintain its functionality and binding affinity for CNTF.
Therapeutic Applications:
The availability of Human Recombinant CNTFR offers potential therapeutic applications in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-mediated signaling presents opportunities to enhance neuronal survival and regeneration, ultimately improving patient outcomes.
Challenges and Future Directions:
While promising, challenges include optimizing the interaction between CNTFR and CNTF, ensuring efficient delivery to target tissues, and understanding potential off-target effects. Ongoing research is essential to unravel the complete mechanisms of CNTFR-mediated signaling and its implications for therapy.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor serves as a crucial tool in advancing our understanding of neuroprotection and regeneration. Its potential to modulate CNTF-mediated effects opens avenues for innovative therapeutic strategies targeting neurodegenerative disorders, exemplifying the intersection of molecular biology and clinical application.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 38.1kDa.

What is the source or expression system of CNTF Protein?
Escherichia Coli.

What is the Purity of CNTF Protein?
CNTF Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.

What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.

What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography tech

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Neurotrophin-1 Human Recombinant, His Tag

Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.

Product # :

CYT-071

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Description

CLCF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (28-225 a.a) and having a molecular mass of 24.6kDa.CLCF1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CLCF1 protein solution (1mg/ml) containing 20mM sodium citrate (pH 3.5), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cardiotrophin-like cytokine factor 1 (CLCF1) is a member of the interleukin 6 family of cytokines, which are involved in cell signaling via phosphorylation of gp130. CLCF1 has a sequence of 225 amino acids with a 27 aa signal peptide, having a molecular mass of 22kDa in the mature form, and the maximum homology to cardiotrophin-1 and ciliary neurotrophic factor. CLCF1 is actively secreted from cells by forming a complex with soluble type I CRLF1 or soluble CNTFR. Defects in the CLCF1 gene cause cold-induced sweating syndrome 2 (CISS2). The CISS2 syndrome is typified by profuse sweating after exposure to cold as well as congenital physical abnormalities of the head and spine.
Synonyms
Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
Background
Cardiotrophin-Like Cytokine Factor 1 Human Recombinant: A Significant Player in Neuronal Development and Immune Regulation
Cardiotrophin-like cytokine factor 1 (CLCF1) has emerged as a crucial player in neuronal development and immune regulation. As a heterodimeric neurotropic cytokine, CLCF1 in complex with cytokine-like factor-1 (CLF-1) has demonstrated vital roles in neuronal development. Studies show that mice lacking this heterodimer exhibit reduced motor neurons and die shortly after birth due to suckling defects. In humans, mutations in the genes encoding for CLCF1 and CLF-1 manifest as Sohar-Crisponi or cold-induced sweating syndrome, with individuals at high risk of early death1.
CLCF1 also exhibits a significant role in the regulation of hematopoiesis, particularly skewing towards myeloid cell differentiation. It has been demonstrated that in mice, CLCF1 promotes B-cell expansion, enhances humoral responses, and triggers autoimmunity. Further, CLCF1 administration resulted in an increase in circulating myeloid cells, along with augmented hematopoietic progenitor cells in the bone marrow. These findings underscore CLCF1's crucial role in modulating the immune system, particularly in the context of bonemarrow transplants and recovery following sub-lethal irradiation2.
Interestingly, CLCF1 is a member of the IL-6 family of cytokines, known for their significant roles in immune regulation and stem cell biology. Like other family members, CLCF1 is secreted as a composite cytokine with CRLF1 and signals through the heterodimerization of the signaling chains LIFRβ and gp130. This suggests overlapping functions with leukemia inhibitor factor (LIF), another IL-6 family member. Expression of CLCF1 is documented in lymph nodes, spleen, and circulating lymphocytes, further establishing its role in immune modulation. However, the comprehensive implications of CLCF1 in immune regulation and hematopoiesis remain an active area of investigation3.
In summary, Cardiotrophin-like cytokine factor 1 human recombinant represents a promising area of research with potential therapeutic implications in neurodevelopmental disorders and immune regulation.
What is the molecular weight/Mw of CLCF Protein?
CLCF Protein has a total Mw of 24.6kDa.

What is the source or expression system of CLCF Protein?
Escherichia Coli.

What is the Purity of CLCF Protein?
CLCF Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CLCF Protein?
The biological functionality of CLCF Protein will be determined in the future.

What is the amino acid sequence of CLCF Protein?
MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

What applications can CLCF Protein be used in?
CLCF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CLCF Protein?
The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniqu

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pigment Epithelium-Derived Factor Human Recombinant

Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

CYT-580

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Description

PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.
Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PEDF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PEDF Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PEDF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
Background
About PEDF Human
Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
several conditions, including heart disease and cancer.
What’s the Function of PEDF Human Recombinant?
PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
only known signaling receptor to be used by a serpin family member.

What’s the Application of PEDF Human Recombinant?
This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
by proprietary chromatographic techniques.
The main purpose of PEDF human recombinant is for research. It has the potential to
become a potential treatment for different angiogenesis-related diseases, including
various cancers. Moreover, it can become crucial during the recovery from vasculature-
related neurodegenerative illness.
Such a discovery could be revolutionary for the world, which is why more research is
needed to determine the effect of this non-inhibitory serpin on the body.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

LIGHT Mouse Recombinant

Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

Product # :

CYT-826

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Description

TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.

Source

Escherichia Coli.

Formulation

TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.

Purity

Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Peroxisomal Biogenesis Factor 26 Human Recombinant

PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

Product # :

PRO-1544

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Description

PEX26 Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-246) and having a molecular mass of 29.3kDa. PEX26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PEX26 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.
Synonyms
PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKSDSST SAAPLRGLGG PLRSSEPVRA VPARAPAVDL LEEAADLLVV HLDFRAALET CERAWQSLAN HAVAEEPAGT SLEVKCSLCV VGIQALAEMD RWQEVLSWVL QYYQVPEKLP PKVLELCILL YSKMQEPGAV LDVVGAWLQD PANQNLPEYG ALAEFHVQRV LLPLGCLSEA EELVVGSAAF GEERRLDVLQ AIHTARQQQK QEHSGSEEAQ KPNLEGSVSH KFLSLPMLVR QLWDSAVSH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cerebral Dopamine Neurotrophic Factor Mouse Recombinant

Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.

Product # :

CYT-729

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Description

CDNF Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.

What is the source or expression system of CDNF Protein?
Escherichia Coli.

What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

What is the amino acid sequence of CDNF Protein?
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.

What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Visfatin Mouse Recombinant

PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

Product # :

CYT-447

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Description

Visfatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-491) containing a 20 aa His tag and having 511 amino acids. The total molecular mass is 57kDa. The Visfatin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution contains 1x PBS pH-7.4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-?, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Physical Appearance
Sterile Filtered colorless 1mg/ml solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECREKKTENSKVR KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERGWNYILEKYDG HLPIEVKAVP EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPITVATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGHDLLHTVFKNGKVTKS YSFDEVRKNA QLNIEQDVAP H.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tumor Necrosis Factor Receptor 2 Fusion Protein Human Recombinant

Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

Product # :

CYT-422

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Shipping Method :

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Description

Recombinant Human Tumor Necrosis Factor Receptor 2 Fusion Protein produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of the extracellular ligand-binding portion of the human 75 kilo Dalton (p75) tumor necrosis factor receptor 2 (TNFR2) linked to the Fc portion of human IgG1. The Fc component of TNFR2 contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. It consists of 934 amino acids and has an apparent molecular weight of approximately 150 kilo Daltons.The TNFR2 is purified by standard chromatographic techniques.

Source

Chinese Hamster Ovarian Cells (CHO).

Formulation

Each mg contains 1.6mg mannitol, 0.4 mg sucrose and 48 µg tromethamine.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.

Biological Activity

Potency is determined by its ability to neutralize TNF-alpha mediated growth inhibition of A375 cells, corresponding to a Specific Activity of 17,000,000 IU/mg.

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Introduction
TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR. Recombinant Human TNFR is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules.
It inhibits the activity of TNF in vitro and has been shown to affect several animal models of inflammation, including murine collagen-induced arthritis. TNFR inhibits binding of both TNF? and TNF? (lymphotoxin alpha [LT?]) to cell surface TNFRs, rendering TNF biologically inactive. Cells expressing transmembrane TNF that bind to TNFR are not lysed in vitro in the presence or absence of complement.
TNFR can also modulate biological responses that are induced or regulated by TNF, including expression of adhesion molecules responsible for leukocyte migration (i.e., E-selectin and to a lesser extent intercellular adhesion molecule-1 [ICAM-1]), serum levels of cytokines (e.g., IL-6), and serum levels of matrix metalloproteinase-3 (MMP-3 or stromelysin).
Synonyms
Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor Receptor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFR2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Ciliary Neurotrophic Factor Receptor Human Recombinant, Sf9

Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha.

Product # :

CYT-1087

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Description

CTNFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 329 amino acids (23-342a.a.) and having a molecular mass of 36.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CTNFR is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CTNFR protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Ciliary Neurotrophic Factor Receptor (CNTFR) is a member of the type I cytokine receptor family and binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
Synonyms
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPQRHSPQE APHVQYERLG SDVTLPCGTA NWDAAVTWRV NGTDLAPDLL NGSQLVLHGL ELGHSGLYAC FHRDSWHLRH QVLLHVGLPPREPVLSCRSN TYPKGFYCSW HLPTPTYIPN TFNVTVLHGS KIMVCEKDPA LKNRCHIRYM HLFSTIKYKV SISVSNALGH NATAITFDEF TIVKPDPPEN VVARPVPSNP RRLEVTWQTP STWPDPESFP LKFFLRYRPL ILDQWQHVEL SDGTAHTITD AYAGKEYIIQ VAAKDNEIGTWSDWSVAAHA TPWTEEPRHL TTEAQAAETT TSTTSSLAPP PTTKICDPGE LGSHHHHHH.
Background
What is the molecular weight/Mw of CNTFR Protein?
CNTFR Protein has a total Mw of 36.9kDa.

What is the source or expression system of CNTFR Protein?
Sf9, Baculovirus cells.
What is the Purity of CNTFR Protein?
CNTFR Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CNTFR Protein?
The biological functionality of CNTFR Protein will be determined in the future.

What is the amino acid sequence of CNTFR Protein?
ADPQRHSPQE APHVQYERLG SDVTLPCGTA NWDAAVTWRV NGTDLAPDLL NGSQLVLHGL ELGHSGLYAC FHRDSWHLRH QVLLHVGLPPREPVLSCRSN TYPKGFYCSW HLPTPTYIPN TFNVTVLHGS KIMVCEKDPA LKNRCHIRYM HLFSTIKYKV SISVSNALGH NATAITFDEF TIVKPDPPEN VVARPVPSNP RRLEVTWQTP STWPDPESFP LKFFLRYRPL ILDQWQHVEL SDGTAHTITD AYAGKEYIIQ VAAKDNEIGTWSDWSVAAHA TPWTEEPRHL TTEAQAAETT TSTTSSLAPP PTTKICDPGE LGSHHHHHH.
What applications can CNTFR Protein be used in?
CNTFR Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CNTFR Protein?
The endotoxin level is minimal, CNTFR Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Ghrelin Human Recombinant

Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.

Product # :

HOR-294

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Description

Ghrelin Human Recombinant contains 115 amino acids (24-117 a.a.) and a total molecular mass of 12.8 kDa. The GHRL is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Ghrelin protein solution contains 20mM Tris-HCl, pH-8 & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
Background
What is the molecular weight/Mw of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein has a total Mw of 12.8kDa.

What is the source or expression system of GHRELIN HUMAN Protein?
Escherichia Coli.

What is the Purity of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GHRELIN HUMAN Protein?
The biological functionality of GHRELIN HUMAN Protein will be determined in the future.

What is the amino acid sequence of GHRELIN HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.

What applications can GHRELIN HUMAN Protein be used in?
GHRELIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GHRELIN HUMAN Protein?
The endotoxin level is minimal, GHRELIN HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Leukemia Inhibitory Factor Mouse Recombinant

CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

Product # :

CYT-645

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Shipped at Room temp

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Description

Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.

Purity

Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CDNF Rat Recombinant

Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.

Product # :

CYT-730

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

CDNF Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.8kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the 6-hydroxy (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.8kDa.

What is the source or expression system of CDNF Protein?
Escherichia Coli.

What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

What is the amino acid sequence of CDNF Protein?
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.

What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic Protein-7 Human Recombinant, His Tag

Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

Product # :

CYT-629

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Quantity :

Shipping Method :

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sds-page

Description

BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.

What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Coagulation Factor IX Human

Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.

Product # :

PRO-353

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Quantity :

Shipping Method :

Shipped at Room temp

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purity
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Description

Human Factor-IX produced from fresh frozen human plasma is a glycosylated polypeptide chain having a molecular mass of 56 kDa.

Source

Human Plasma.

Formulation

The Factor-IX was lyophilized from a sterile solution containing 20mM Tris-HCl pH-7.4, 0.1M NaCl and 1mM Benzamidine.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity per mg was tested and found to be 306.5 PEU/mg.

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Introduction
Human Factor IX also called Christmas-Factor is a glycoprotein, which is synthesized in the liver and belongs to the serine proteases system and is part of the S1 peptidase family.
Lack of Factor-IX causes Hemophilia-B meaning Christmas Disease. Factor-IX has a N-terminus region which contains 12xGla residues which asist the calcium dpendant binding of Factor-IX to the phospholipid surface. Factor-IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage yields the intermediate IXa, which is subsequently converted to the fully active form IXab.
Factor-IX binds initially to exosites on the factor XIa heavy chain, followed by interaction at the active site with subsequent bond cleavage. Coagulation factor IX is activated by interaction with the erythrocyte membrane, causing intrinsic coagulation. Chaperones & lectins act simultaniously to guarantee the proper folding of Factor-IX and the retention of mutant molecules. Human Factor IX, activated by either the Contact or Tissue Factor Pathway, is responsible for the activation of Factor X to Xa.
Synonyms
Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Factor-IX although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-IX should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized 100U Factor-IX in sterile 100µl of 18MΩ-cm H2O, which can then be further diluted to other aqueous solutions.
Human Virus Test
Human plasma was tested and found negative for HIV-1, HIV-2, Hepatitis B Surface antigen and HCV. Donors are screened for CJD (Creutzfeldt-Jakob Disease).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Precursor Brain-Derived Neurotrophic Factor Human Recombinant

proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

Product # :

CYT-014

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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purity
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Description

proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.
Synonyms
proBDNF, Precursor Form Brain-derived Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized proBDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.
Background
Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor
Abstract:
Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.
Introduction:
Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.
Characteristics and Processing Mechanisms:
proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.
Production of proBDNF Human Recombinant:
Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.
Potential Therapeutic Applications:
proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.
Conclusion:
proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 52kDa.

What is the source or expression system of BDNF Protein?
Escherichia Coli.

What is the Purity of BDNF Protein?
BDNF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BDNF Protein?
The biological functionality of BDNF Protein will be determined in the future.

What is the amino acid sequence of BDNF Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Kruppel-Like Factor 7 Human Recombinant

UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

Product # :

PRO-1527

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Description

KLF7 Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-302) and having a molecular mass of 35.8kDa. KLF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The KLF7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Kruppel-Like Factor 7 (KLF7) is a part of the Kruppel-like transcriptional regulator family whose members regulate cell proliferation, differentiation and survival and contain 3 C2H2 zinc fingers at the C-terminus that mediate binding to GC-rich sites. KLF7 contributes to the progression of type 2 diabetes by inhibiting hormone expression and secretion in pancreatic beta-cells and also by deregulating adipocytokine secretion in adipocytes.
Synonyms
UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDVLASY SIFQELQLVH DTGYFSALPS LEETWQQTCL ELERYLQTEP RRISETFGED LDCFLHASPP PCIEESFRRL DPLLLPVEAA ICEKSSAVDI LLSRDKLLSE TCLSLQPASS SLDSYTAVNQ AQLNAVTSLT PPSSPELSRH LVKTSQTLSA VDGTVTLKLV AKKAALSSVK VGGVATAAAA VTAAGAVKSG QSDSDQGGLG AEACPENKKR VHRCQFNGCR KVYTKSSHLK AHQRTHTGEK PYKCSWEGCE WRFARSDELT RHYRKHTGAK PFKCNHCDRC FSRSDHLALH MKRHI.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Leukemia Inhibitory Factor Human Recombinant, Sf9

Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

Product # :

CYT-1003

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Description

LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

LIF protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
QAFHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cerebral Neurotrophic Factor Human Recombinant

Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

Product # :

CYT-167

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Description

CDNF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L
Background
Cerebral Neurotrophic Factor Human Recombinant: A Leap Forward in Neurobiology
The field of neurobiology is replete with wonder, particularly due to the influential role of neurotrophic factors. These essential proteins, responsible for the survival and growth of neurons, have become a focal point in modern research. Among these, the Cerebral Neurotrophic Factor (CNF) stands out, offering novel insights and potential breakthroughs in our understanding of neurological health.
Enter the world of bioengineering, a scientific arena where we have successfully replicated CNF, leading to the birth of Cerebral Neurotrophic Factor Human Recombinant (CNF-HR). This is a massive step towards conquering neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, conditions that have perplexed scientists and clinicians for decades.
The extraordinary capacity of CNF-HR lies in its dual functionality - it acts as a defender and a promoter. It defends neurons from harmful degenerative processes while promoting their growth and development. Picture a devoted gardener who tirelessly protects his garden from pests and nurtures the growth of each plant. In this context, the brain is the vibrant garden, and the neurons, the delicate plants we must care for.
Although this scientific breakthrough sparks enthusiasm, it's crucial to remember the challenges that lie ahead. The path to determining the most effective method of delivering CNF-HR to the brain, identifying the optimal dosage, and monitoring potential side effects is a winding one. Nevertheless, with continuous research and relentless scientific curiosity, we are optimistic about overcoming these challenges.
In conclusion, the development of CNF-HR is a significant milestone in the fascinating journey of neurobiology. Its potential to change the trajectory of treating neurodegenerative diseases and enhancing our understanding of neuronal function is tremendous. While the journey is strewn with complexities, the potential rewards we stand to reap promise a future where neurodegenerative diseases could be effectively managed or even cured.
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.

What is the source or expression system of CDNF Protein?
Escherichia Coli.

What is the Purity of CDNF Protein?
CDNF Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

What is the amino acid sequence of CDNF Protein?
QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF Protein was purified using conventional chromatography techniques

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pigment Epithelium-Derived Factor Human Recombinant, HEK

Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

Product # :

CYT-553

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Description

PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recomnded to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

General Transcription Factor IIA, 1 Human Recombinant

General transcription factor IIA, 1, 19/37kDa, TF2A1, TFIIA, TFIIA-42, TFIIAL, Transcription initiation factor IIA subunit 1, Transcription initiation factor TFIIA 42 kDa subunit, GTF2A1.

Product # :

PRO-1808

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Description

GTF2A1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 32.2kDa. GTF2A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GTF2A1 solution (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
General Transcription Factor IIA, 1 (GTF2A1) in a complex along with TBP mediates transcriptional activity. GTF2A1 is a part of the transcription machinery of RNA polymerase II and is also participates in transcriptional activation.
Synonyms
General transcription factor IIA, 1, 19/37kDa, TF2A1, TFIIA, TFIIA-42, TFIIAL, Transcription initiation factor IIA subunit 1, Transcription initiation factor TFIIA 42 kDa subunit, GTF2A1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMANSANT NTVPKLYRSV IEDVINDVRD IFLDDGVDEQ VLMELKTLWE NKLMQSRAVD GFHSEEQQLL LQVQQQHQPQ QQQHHHHHHH QQAQPQQTVP QQAQTQQVLI PASQQATAPQ VIVPDSKLIQ HMNASNMSAA ATAATLALPA GVTPVQQILT NSGQLLQVVR AANGAQYIFQ PQQSVVLQQQ VIPQMQPGGV QAPVIQQVLA PLPGGISPQT GVIIQPQQIL FTGNKTQVIP TTVAAPTPAQ AQITATGQQQ PQAQPAQTQA PLVLQVD.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tumor Necrosis Factor-Alpha Mouse Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-252

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Shipped at Room temp

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Description

Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000Units/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Hormone-1, Mouse Anti Human

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

ANT-230

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% sodium azide.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered solution.
Immunogen
GH Antibody is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant Growth hormone.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PG3H5AT.
Applications
The GH antibody has been tested by ELISA and by Western blot analysis to assure specificity and reactivity. Since application vary, however, each investigation should titrate the reagent to obtain optimal results. Recommended dilution range for Western blot analysis: 1:500 ~ 1:1000. Recommended starting dilution: 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4 C, for longer periods of time, store at -20 C. Prevent freeze thaw cycles.
Purification Method
GH antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Sonic HedgeHog Human Recombinant

SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

Product # :

CYT-676

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Description

Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.

Source

Escherichia Coli.

Formulation

SHH is lyophilized from 10mM Na3PO4, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.

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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized SHH in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-6 Mouse Recombinant, Sf9

Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.

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CYT-904

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Description

Interleukin-6 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 193 amino acids (25-211a.a.) and having a molecular mass of 22.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL 6 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED₅₀ for this effect is less or equal to 0.1 ng/ml.

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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
Synonyms
Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQTHHH HHH.
Background
Research Paper on Interleukin-6 Mouse Recombinant, Sf9
Abstract:
Exploring Interleukin-6 Mouse Recombinant, Sf9, a fascinating research topic! This paper provides an extensive description of Interleukin-6 (IL-6) Mouse Recombinant expressed in Sf9 insect cells. We delve into the molecular properties of IL-6, its significance in immune responses and inflammation, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 research using this novel recombinant mouse protein.
Introduction:
Introducing Interleukin-6 Mouse Recombinant, Sf9. This paper sheds light on the production and characteristics of IL-6 expressed in Sf9 insect cells. As researchers, we are intrigued by the versatility and applications of this recombinant protein in immunological studies.
An Extensive Description of Interleukin-6 Mouse Recombinant:
We present a comprehensive overview of Interleukin-6 Mouse Recombinant, focusing on its structure and functions. This recombinant protein enables us to explore IL-6's role in various cellular processes, making it a valuable tool for investigating immune regulation.
Significance in Immune Responses:
Marvel at IL-6's critical role in orchestrating immune responses! As a key cytokine, IL-6 plays a central role in immune cell activation and the regulation of inflammatory processes. Its pleiotropic effects contribute to maintaining homeostasis in the immune system.
Interactions and Synonyms:
Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our understanding of the interconnectedness of cytokine signaling. The complex interactions between IL-6 and other molecules further enrich our knowledge of immune responses.
Potential Applications in Immunological Research:
Explore the wide range of applications of Interleukin-6 Mouse Recombinant in immunological studies. From cell-based assays to therapeutic developments, this recombinant protein offers novel avenues for advancing immunology research. It serves as a valuable tool in deciphering the intricate immune system functions.
Novel Production Method using Sf9 Insect Cells:
Discover the innovative use of Sf9 insect cells for producing Interleukin-6. This expression system provides a scalable and efficient approach for obtaining large quantities of functional IL-6. The use of Sf9 cells opens up possibilities for large-scale protein production and downstream applications.
Conclusion:
Concluding our exploration of Interleukin-6 Mouse Recombinant, Sf9, we recognize its significance in immunological research. The extensive description of this recombinant protein broadens our understanding of IL-6 biology and its potential applications in various fields. As researchers, we are excited about the potential discoveries that lie ahead with the help of this valuable tool.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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