Search: 1000 results found for "manf"

Description:

NTF2-like Export Factor 1 Human Recombinant

NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.

Product # :

PRO-218

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Description

NXT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140a.a.) and having a molecular mass of 18.0kDa. The NXT1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NXT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol and 0.1M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
NXT1 operates as a nuclear export factor in both RAN and CRM1 dependent pathways. NXT1 is known to stimulate the export of U1 snRNA in RAN (Ras-related nuclear protein) and CRM1 (chromosome region maintenance) dependent pathways and the export of tRNA and mRNA in a CRM1-independent pathway. This protein heterodimerizes with Tap protein and regulates the ability of Tap protein to intermediate nuclear mRNA export.
Synonyms
NTF2-like export factor 1, MTR2, Protein P15, NTF2-related export protein 1, NUTF-like export factor 1, NTX2-like export factor1.
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 MASVDFKTYV DQACRAAEEF VNVYYTTMDK RRRLLSRLYM GTATLVWNGN AVSGQESLSE FFEMLPSSEF QISVVDCQPV HDEATPSQTT VLVVICGSVK FEGNKQRDFN QNFILTAQAS PSNTVWKIAS DCFRFQDWAS.

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:

Apo Transferrin Human

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

Product # :

PRO-325

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Description

Human Apo Transferrin is a glycoprotein of approximately 77 kDa.

Source

Human serum.

Formulation

The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.

Purity

Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.

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:

Nerve Growth Factor Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.

Product # :

CYT-915

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Description

NGFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 230 amino acids (29-250 a.a.) and having a molecular mass of 24.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). NGFR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 16 (NGFR) BELONGS TO the tumor necrosis factor receptor superfamily with an extensive pattern of expression in tissues such as the brain, liver, lung, and muscle. NGFR has a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, possibly by regulating RAB31 activity, and thus contributes to the regulation of insulin-dependent glucose uptake. NGFRs are low affinity receptors which can bind to NGF, BDNF, NT-3, and NT-4. NGFR mediates cell survival as well as cell death of neural cells.
Synonyms
Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.
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
KEACPTGLYT HSGECCKACN LGEGVAQPCG ANQTVCEPCL DSVTFSDVVS ATEPCKPCTE CVGLQSMSAP CVEADDAVCR CAYGYYQDET TGRCEACRVC EAGSGLVFSC QDKQNTVCEE CPDGTYSDEA NHVDPCLPCT VCEDTERQLR ECTRWADAEC EEIPGRWITR STPPEGSDST APSTQEPEAP PEQDLIASTV AGVVTTVMGS SQPVVTRGTT DNLEHHHHHH.

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:

Glia Maturation Factor Gamma Human Recombinant

Glia maturation factor gamma, GMF-gamma, GMFG, MGC126867.

Product # :

CYT-632

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Description

Glia Maturation Factor-Gamma (GMF-Gamma) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 142 amino acids and having a total molecular mass of 16.8 kDa. Glia Maturation Factor-Gamma, GMF-Gamma, Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GMF-gamma protein contains 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
GMFG is a hematopoietic-specific protein that mediates the pluripotentiality and lineage commitment of human hematopoietic stem cells. Glia maturation factor gamma is a cytokine-responsive protein in EPO-induced and G-CSF-induced hematopoietic lineage development. Glia maturation factor also acts as a Nerve Growth Factor in nervous system development, angiogenesis and immune function. GMFG possesses hematopoietic tissue-specific gene expression, a promoter concentrated with high-score hematopoiesis-specific transcription factors, and molecular coevolution with a rudimentary blood/immune system.
Synonyms
Glia maturation factor gamma, GMF-gamma, GMFG, MGC126867.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ
QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR.
Background
What is the molecular weight/Mw of GMFG HUMAN Protein?
GMFG HUMAN Protein has a total Mw of 16.8kDa.

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

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

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

What is the amino acid sequence of GMFG HUMAN Protein?
MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ
QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR.

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

What is the endotoxin level for GMFG HUMAN Protein?
The endotoxin level is minimal, GMFG 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:

Neudesin Neurotrophic Factor Human Recombinant

Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

Product # :

CYT-778

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Description

NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.

Source

Escherichia Coli.

Formulation

NENF was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.
Synonyms
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
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; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. NENF is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.

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:

Pro-Nerve Growth Factor Human Recombinant

Human Pro-NGF, ProNGF, NGFB.

Product # :

CYT-426

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Description

Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Human Pro-NGF, ProNGF, NGFB.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF 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 ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA.
Background
Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis
Abstract:
Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.
Introduction:
Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.
Characteristics and Processing Mechanisms:
Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.
Production and Manipulation of Pro-NGF Human Recombinant:
Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.
Implications in Neuroregulation and Disease Pathogenesis:
Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.
Conclusion:
Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.
What is the molecular weight / Mw of ProNGF Protein?
ProNGF Protein has a total Mw of 25kDa.

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

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

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

What is the amino acid sequence of ProNGF Protein?
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA

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

What is the endotoxin level for ProNGF Protein?
The endotoxin level is minimal, ProNGF 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:

Mago-Nashi Homolog Human Recombinant

MAGOH1, MAGOHA, Protein mago nashi homolog, MAGOH, proliferation-associated (Drosophila).

Product # :

PRO-810

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Description

MAGOH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-146 a.a.) and having a molecular mass of 18.2 kDa. MAGOH protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

MAGOH Human solution containing 20mM Tris-HCl pH-8, 2mM DTT, 0.1M NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Drosophila that have mutations in their MAGOH gene produce progeny with defects in germplasm assembly and germline development. MAGOH, the human homolog of Drosophila mago nashi, is necessary for embryo development. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and is induced by serum stimulation of quiescent fibroblast.
Synonyms
MAGOH1, MAGOHA, Protein mago nashi homolog, MAGOH, proliferation-associated (Drosophila).
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
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT TSKIGSLIDV NQSKDPEGLR VFYYLVQDLK CLVFSLIGLH FKIKPILEHH HHHH.

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:

GDNF Family Receptor Alpha 1 Human Recombinant

GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

Product # :

CYT-1026

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Shipped at Room temp

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Description

GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).

Source

HEK293 cells.

Formulation

GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
Synonyms
GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.
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; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. GFRA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.
Background
What is the molecular weight/Mw of GFRA1 Protein?
GFRA1 Protein has a total Mw of 46kDa.

What is the source or expression system of GFRA1 Protein?
HEK293 cells.
What is the Purity of GFRA1 Protein?
GFRA1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA1 Protein?
The biological functionality of GFRA1 Protein will be determined in the future.

What is the amino acid sequence of GFRA1 Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

What applications can GFRA1 Protein be used in?
GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA1 Protein?
The endotoxin level is minimal, GFRA1 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:

Activating Transcription Factor-1 Human Recombinant

Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.

Product # :

PKA-019

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Description

ATF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-271 and having a molecular mass of 31.8kDa.ATF1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ATF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.
Synonyms
Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-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
MGSSHHHHHH SSGLVPRGSH MGSHMEDSHK STTSETAPQP GSAVQGAHIS HIAQQVSSLS ESEESQDSSD SIGSSQKAHG ILARRPSYRK ILKDLSSEDT RGRKGDGENS GVSAAVTSMS VPTPIYQTSS GQYIAIAPNG ALQLASPGTD GVQGLQTLTM TNSGSTQQGT TILQYAQTSD GQQILVPSNQ VVVQTASGDM QTYQIRTTPS ATSLPQTVVM TSPVTLTSQT TKTDDPQLKR EIRLMKNREA ARECRRKKKE YVKCLENRVA VLENQNKTLI EELKTLKDLY SNKSV

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:

Mannoside Acetylglucosaminyltransferase 2 Human Recombinant

Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

Product # :

ENZ-781

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Description

MGAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (30-447a.a) and having a molecular mass of 50kDa. MGAT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MGAT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Mannoside Acetylglucosaminyltransferase 2 (MGAT2) is a golgi enzyme catalyzing an vital step in the conversion of oligomannose to complex N-glycans. MGAT2 enzyme has the characteristic glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. MGAT2 gene mutations may lead to carbohydrate-deficient glycoprotein syndrome, type II.
Synonyms
Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRQRKNEALA PPLLDAEPAR GAGGRGGDHP SVAVGIRRVS NVSAASLVPA VPQPEADNLT LRYRSLVYQL NFDQTLRNVD KAGTWAPREL VLVVQVHNRP EYLRLLLDSL RKAQGIDNVL VIFSHDFWST EINQLIAGVN FCPVLQVFFP FSIQLYPNEF PGSDPRDCPR DLPKNAALKL GCINAEYPDS FGHYREAKFS QTKHHWWWKL HFVWERVKIL RDYAGLILFL EEDHYLAPDF YHVFKKMWKL KQQECPECDV LSLGTYSASR SFYGMADKVD VKTWKSTEHN MGLALTRNAY QKLIECTDTF CTYDDYNWDW TLQYLTVSCL PKFWKVLVPQ IPRIFHAGDC GMHHKKTCRP STQSAQIESL LNNNKQYMFP ETLTISEKFT VVAISPPRKN GGWGDIRDHE LCKSYRRLQ.

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

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.

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:

Macrophage Colony Stimulating Factor Human Recombinant, Sf9

Macrophage colony-stimulating factor 1, CSF-1, M-CSF, MCSF, Lanimostim.

Product # :

CYT-1015

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Description

MCSF produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 231 amino acids (33-255 a.a.) and having a molecular mass of 26.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).MCSF is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cell. The ED50 for this effect is less or equal to 3 ng/ml.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
Macrophage colony-stimulating factor 1, CSF-1, M-CSF, MCSF, Lanimostim.
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
EEVSEYCSHM IGSGHLQSLQ RLIDSQMETS CQITFEFVDQ EQLKDPVCYL KKAFLLVQDI MEDTMRFRDN TPNAIAIVQL QELSLRLKSC FTKDYEEHDK ACVRTFYETP LQLLEKVKNV FNETKNLLDK DWNIFSKNCN NSFAECSSQD VVTKPDCNCL YPKAIPSSDP ASVSPHQPLA PSMAPVAGLT WEDSEGTEGS SLLPGEQPLH TVDPGSAKQR PPRLEHHHHH 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:

Epidermal Growth Factor Receptor Human Recombinant Sf9, Active

Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

Product # :

PKA-335

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Description

EGFR Human Recombinant encoding a.a. 672-1210 expressed in Baculovirus infected Sf9 cells, fused with a GST-tag at N-terminus with thrombin cleavage sites, having a molecular weight of 89,171 Dalton.EGFR is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Sf9 cells.

Formulation

EGFR in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT, 15mM reduced glutathione and 20% glycerol.

Biological Activity

Determination of Km value by Filter binding assay MAFC membrane.

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Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Physical Appearance
Sterile filtered liquid.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please avoid freeze-thaw cycles.
Specific Activity
30 pmol/µgxmin.

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:

Myeloid Leukemia Factor 1 Human Recombinant

Myeloid leukemia factor 1, Myelodysplasia-myeloid leukemia factor 1, MLF1.

Product # :

PRO-100

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Description

MLF1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 288 amino acids (1-268 a.a.) and having a molecular mass of 32.8kDa (Molecular weight on SDS-PAGE will appear higher). The MLF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MLF1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 5mM DTT and 200mM NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Myeloid leukemia factor 1 (MLF1) is a member of the MLF family, and is a widely expressed negative regulator of cell cycle progression functioning upstream of the tumor suppressor p53. MLF1 hinders the erythropoietin-induced erythroid terminal differentiation by averting cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. MLF1 generally functions in multi-potent progenitor cells, and its dysregulation may be to some extent responsible for leukemogenesis. Translocations between the MLF1 gene and nucleophosmin are linked to myelodysplastic syndrome and acute myeloid leukemia.
Synonyms
Myeloid leukemia factor 1, Myelodysplasia-myeloid leukemia factor 1, MLF1.
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 MFRMLNSSFE DDPFFSESIL AHRENMRQMI RSFSEPFGRD LLSISDGRGR AHNRRGHNDG EDSLTHTDVS SFQTMDQMVS NMRNYMQKLE RNFGQLSVDP NGHSFCSSSV MTYSKIGDEP PKVFQASTQT RRAPGGIKET RKAMRDSDSG LEKMAIGHHI HDRAHVIKKS KNKKTGDEEV NQEFINMNES DAHAFDEEWQ SEVLKYKPGR HNLGNTRMRS VGHENPGSRE LKRREKPQQS PAIEHGRRSN VLGDKLHIKG SSVKSNKK.

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:

Holo Transferrin Human

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

Product # :

PRO-315

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Description

Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

Source

Human serum.

Formulation

The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
May contain traces of buffer salts.

Purity

Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.
Iron Content
The Iron content was estimated by ICP and was found to be 1232 ppm.

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:

Myostatin Propeptide Human Recombinant

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-448

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Description

Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.

Source

Escherichia Coli.

Formulation

Lyophilized with no additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.

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Introduction
Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
Sterile 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 recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.

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:

beta Nerve Growth Factor Human Recombinant, HEK

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-079

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Description

BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.

Source

HEK293 cells.

Formulation

The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.

Purity

Greater than 97% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED₅₀ is <0.04-0.4ng/ml.

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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF 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 b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.

What is the source or expression system of B NGF Protein?
HEK293 cells.

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

What is the Biological Activity of B NGF Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.

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

What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF 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:

Mitochondrial Antiviral Signaling Protein Human Recombinant

CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

Product # :

PRO-1351

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Description

MAVS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 536 amino acids (1-513) and having a molecular mass of 55.9 kDa. MAVS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAVS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Mitochondrial antiviral signaling protein (MAVS) is vital for innate immune defense against viruses. MAVS is an intermediary protein essential in the virus-triggered IFN-beta signaling pathways. MAVS is involved in activation of transcription factors that regulate expression of IFN-beta and contributes to antiviral immunity.
Synonyms
CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.
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 MGSMPFAEDK TYKYICRNFS NFCNVDVVEI LPYLPCLTAR DQDRLRATCT LSGNRDTLWH LFNTLQRRPG WVEYFIAALR GCELVDLADE VASVYQSYQP RTSDRPPDPL EPPSLPAERP GPPTPAAAHS IPYNSCREKE PSYPMPVQET QAPESPGENS EQALQTLSPR AIPRNPDGGP LESSSDLAAL SPLTSSGHQE QDTELGSTHT AGATSSLTPS RGPVSPSVSF QPLARSTPRA SRLPGPTGSV VSTGTSFSSS SPGLASAGAA EGKQGAESDQ AEPIICSSGA EAPANSLPSK VPTTLMPVNT VALKVPANPA SVSTVPSKLP TSSKPPGAVP SNALTNPAPS KLPINSTRAG MVPSKVPTSM VLTKVSASTV PTDGSSRNEE TPAAPTPAGA TGGSSAWLDS SSENRGLGSE LSKPGVLASQ VDSPFSGCFE DLAISASTSL GMGPCHGPEE NEYKSEGTFG IHVAENPSIQ LLEGNPGPPA DPDGGPRPQA DRKFQEREVP CHRPSP.

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:

BAFF (BLyS) Receptor Human Recombinant, HEK

TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

Product # :

CYT-1224

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Description

BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

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Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
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
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.
Background
B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.
Structural Architecture of BAFF Receptor Protein:
BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.
Physiological Significance in B-Cell Biology:
BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.
Regulation of Immune Responses:
BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.
BAFF Receptor as a Therapeutic Target:
The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.
BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.
What is the molecular weight/Mw of BAFF-R Protein?
BAFF-R Protein has a total Mw of 34.4kDa.

What is the source or expression system of BAFF-R Protein?
HEK293 Cells.

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

What is the Biological Activity of BAFF-R Protein?
The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

What is the amino acid sequence of BAFF-R Protein?
DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

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

What is the endotoxin level for BAFF-R Protein?
The endotoxin level is minimal, BAFF-R 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:

Epidermal Growth Factor Long Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-798

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Shipped at Room temp

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Description

Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.

Purity

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

Biological Activity

The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.

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

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

What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

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

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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:

Tumor Necrosis Factor-alpha Human Recombinant, Sf9

Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

Product # :

CYT-903

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Description

TNF a produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 163 amino acids (77-233a.a.) and having a molecular mass of 18.1kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TNF a is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNF a protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined bySDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.

The ED50 for this effect is ≤ 0.2 ng/ml.

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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
Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIALHHH HHH.

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:

Mago-Nashi Homolog B Human Recombinant

mago-nashi homolog B (Drosophila), mago, magoh, MGN2, MAGOHB, MAGOH2.

Product # :

PRO-1488

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Description

MAGOHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-148 a.a.) and having a molecular mass of 19.7kDa.MAGOHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MAGOHB protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 1mM DTT, 30% glycerol and 0.15M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Mago-Nashi Homolog B (MAGOHB) is a member of the mago nashi family. MAGOHB involved in mRNA splicing and in the nonsense-mediated decay (NMD) pathway. MAGOHB interacts with RBM8A and is a part of the exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, UPF3B, UPF2 and ALYREF/THOC4.
Synonyms
mago-nashi homolog B (Drosophila), mago, magoh, MGN2, MAGOHB, MAGOH2.
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 MGSMAVASDF YLRYYVGHKG KFGHEFLEFE FRPDGKLRYA NNSNYKNDVM IRKEAYVHKS VMEELKRIID DSEITKEDDA LWPPPDRVGR QELEIVIGDE HISFTTSKIG SLIDVNQSKD PEGLRVFYYL VQDLKCLVFS LIGLHFKIKP I.

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:

MYC Associated Factor X Human Recombinant

bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.

Product # :

PRO-811

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Description

MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

MAX Human solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.
Synonyms
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
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
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.

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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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.

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