Search: 1000 results found for "cdnf"

Description:

Colony Stimulating Factor 1 Receptor Human Recombinant

Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS.

Product # :

CYT-1068

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Description

MCSFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 737 amino acids (20-517a.a.) and having a molecular mass of 82.1kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MCSFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MCSFR 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 by its ability to inhibit M-CSF dependent proliferation of M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is less or equal to 100ng/ml in the presence of 10 ng/ml M-CSF.

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Introduction
MCSFR which is also familiar as CSF1R, is part of the type3 subfamily of receptor tyrosine kinases. MCSFR is expressed mainly on cells of the monocyte and macrophage lineage, stem cells, and in the growing placenta. Most of the biological effects of this cytokine are mediated by MCSFR. MCSFR contains an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Originally CSF1 and this receptor were implicated as vital for normal trophoblastic implantation as well as monocyte development. The role of CSF1/CSF1R in normal mammary gland development is actually very interesting since this connection has also been discovered in the biology of breast cancer with the results of abnormal expression of CSF1 and its receptor. Likewise, in Alzheimer's disease and after brain injuries an increased level of CSF1R was found in the microglia, which causes the microglia to become more active.
Synonyms
Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS.
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
IPVIEPSVPE LVVKPGATVT LRCVGNGSVE WDGPPSPHWT LYSDGSSSIL STNNATFQNT GTYRCTEPGD PLGGSAAIHL YVKDPARPWN VLAQEVVVFE DQDALLPCLL TDPVLEAGVS LVRVRGRPLM RHTNYSFSPW HGFTIHRAKF IQSQDYQCSA LMGGRKVMSI SIRLKVQKVI PGPPALTLVP AELVRIRGEA AQIVCSASSV DVNFDVFLQH NNTKLAIPQQ SDFHNNRYQK VLTLNLDQVD FQHAGNYSCV ASNVQGKHST SMFFRVVESA YLNLSSEQNL IQEVTVGEGL NLKVMVEAYP GLQGFNWTYL GPFSDHQPEP KLANATTKDT YRHTFTLSLP RLKPSEAGRY SFLARNPGGW RALTFELTLR YPPEVSVIWT FINGSGTLLC AASGYPQPNV TWLQCSGHTD RCDEAQVLQV WDDPYPEVLS QEPFHKVTVQ SLLTVETLEH NQTYECRAHN SVGSGSWAFI PISAGAHTHP PDEFLFTPLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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:

Complement Factor D Human

Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.

Product # :

PRO-2699

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Description

Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.

Source

Human Plasma.

Formulation

CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.
Synonyms
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
Physical Appearance
Sterile filtered solution.
Stability
CFD Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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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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:

Tumor Necrosis Factor Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, Tumor necrosis factor receptor type I, TNF-R1, TNF-RI, TNFR-I, p60, p55, CD120a, TNFRSF1A, TNFAR, TNFR1, FPF, TBP1, TNF-R, p55-R, TNFR55, TNFR60, TNF-R-I, TNF-R55, MGC19588.

Product # :

CYT-707

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Description

TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids and having a total molecular mass of 18.2 kDa. TNFR Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TNFR protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.

Purity

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

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Introduction
TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.
Synonyms
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, Tumor necrosis factor receptor type I, TNF-R1, TNF-RI, TNFR-I, p60, p55, CD120a, TNFRSF1A, TNFAR, TNFR1, FPF, TBP1, TNF-R, p55-R, TNFR55, TNFR60, TNF-R-I, TNF-R55, MGC19588.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFR although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR should be stored at 4C between 2-7 days and for future use below -18C. 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 TNFR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDSVCPQGKY IHPQNNSICC TKCHKGTYLY NDCPGPGQDT DCRECESSGSF TASENHLRHC LSCSKCRKEM GQVEKSSCTV DRDTVCGCRK NQYRHYWSEN LFQCFNCSLC LNGTVHLSCQ EKQNTVCTCH AGFFLRENEC VSCSNCKKSL ECTKLCLPQI EN.

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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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:

Cysteine-Rich Angiogenic Inducer 61 Human Recombinant

CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

Product # :

CYT-164

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Description

CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

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Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 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 CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:

Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.
Introduction:

Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.
Production and Characterization:

Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.
Role in Angiogenesis:

CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.
Therapeutic Implications:

The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.
Conclusion:

Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.
What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.

What is the source or expression system of CCN1 Protein?
Escherichia Coli.

What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD

What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 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:

CD30 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.

Product # :

CYT-824

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Description

TNFSF8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (63-234 a.a.) and having a molecular mass of 22kDa.TNFSF8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFSF8 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
Synonyms
Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.
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 MGSQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSD.

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:

Canopy FGF Signaling Regulator 1 Human Recombinant

Protein canopy homolog 1, CNPY1.

Product # :

PRO-1872

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Description

CNPY1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-92 a.a) and having a molecular mass of 13.3kDa. CNPY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNPY1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Canopy FGF Signaling Regulator 1, also known as CNPY1, is expressed in the midbrain-hindbrain (MHB) boundary in zebrafish. CNPY1, which binds FGFR1, also takes part in FGF signaling.
Synonyms
Protein canopy homolog 1, CNPY1.
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 MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL.

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:

GM-CSF Receptor Alpha Human Recombinant

CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

Product # :

CYT-796

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Description

CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
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.
Background
Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.
Therapeutic Applications:
Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.
Challenges and Future Directions:
While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 37.2kDa.

What is the source or expression system of CD116 Protein?
Escherichia Coli.

What is the Purity of CD116 Protein?
CD116 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
The biological functionality of CD116 Protein will be determined in the future.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 324 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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:

Granulocyte Macrophage-Colony Stimulating Factor Rhesus Macaque Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Product # :

CYT-720

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Description

Granulocyte Macrophage Colony Stimulating Factor Monkey Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.4 kDa.GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH 7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE and RP-HPLC.

Biological Activity

The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 IU/mg.

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13. GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APARSPSPGT QPWEHVNAIQ EARRLLNLSR DTAAEMNKTV EVVSEMFDLQ EPSCLQTRLE LYKQGLQGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQI ITFQSFKENL KDFLLVIPFD CWEPVQE.

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 3 Human Recombinant, Sf9

GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.

Product # :

CYT-1013

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Description

GFRA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (32-374) and having a molecular mass of 65.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GFRA3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.
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
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
Background
What is the molecular weight/Mw of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein has a total Mw of 65.5kDa.

What is the source or expression system of GFRA3 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA3 HUMAN, SF9 Protein?
The biological functionality of GFRA3 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of GFRA3 HUMAN, SF9 Protein?
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

What applications can GFRA3 HUMAN, SF9 Protein be used in?
GFRA3 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA3 HUMAN, SF9 Protein?
The endotoxin level is minimal, GFRA3 HUMAN, SF9 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:

Cardiotrophin-1 Human Recombinant

CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

Product # :

CYT-944

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Description

Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.The CTF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CTF-1 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

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 human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ IU/mg.

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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.
Synonyms
CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF-1 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.
Background
Title: Cardiotrophin-1 Human Recombinant: A Potential Therapeutic Target for Cardiovascular Diseases
Abstract:

Cardiotrophin-1 (CT-1) is a cytokine that plays a crucial role in cardiac development and homeostasis. This research paper provides a comprehensive analysis of human recombinant CT-1, focusing on its production, characterization, and potential therapeutic implications in cardiovascular diseases. The paper discusses the significance of CT-1 in cardiac cell survival, hypertrophy, and regeneration. Furthermore, it elucidates the ongoing research and clinical trials exploring the therapeutic potential of recombinant CT-1 in cardiovascular disorders. The information presented in this paper aims to enhance the understanding of human recombinant CT-1 and its utility as a research tool and a potential therapeutic agent for cardiovascular diseases.
Introduction:

Cardiotrophin-1 (CT-1) is a member of the interleukin-6 cytokine family, primarily produced by cardiac cells. It exerts its effects by binding to the CT-1 receptor complex, leading to the activation of various signaling pathways. Human recombinant CT-1, produced through genetic engineering techniques, provides researchers with a valuable tool to explore its biological functions and therapeutic potential.
Production and Characterization:

Recombinant CT-1 is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CT-1.
Role in Cardiovascular Physiology:

CT-1 plays a critical role in cardiac cell survival, hypertrophy, and regeneration. It promotes cardiomyocyte growth and survival, contributing to the adaptation of the heart to stress and injury. CT-1 also exhibits angiogenic properties, stimulating the formation of new blood vessels in the heart. These functions make recombinant CT-1 an important tool for studying cardiac physiology and exploring potential therapeutic interventions.
Therapeutic Implications:

The dysregulation of CT-1 signaling has been implicated in various cardiovascular diseases, including heart failure, myocardial infarction, and cardiac hypertrophy. Recombinant CT-1 holds promise as a potential therapeutic agent for these conditions. Clinical trials are underway to evaluate the safety and efficacy of CT-1-based therapies, including recombinant CT-1 administration and gene therapy approaches.
Conclusion:

Human recombinant CT-1 is a valuable research tool and a potential therapeutic target for cardiovascular diseases. Its production, characterization, and applications in cardiac cell signaling contribute to our understanding of cardiovascular physiology and the development of novel treatments. Continued research and clinical trials exploring the therapeutic potential of recombinant CT-1 hold promise for improving outcomes in patients with cardiovascular disorders.
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.2kDa.

What is the source or expression system of CTF1 Protein?
Escherichia Coli.

What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF1 Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 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 CTF1 Protein?
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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:

Canopy FGF Signaling Regulator 4 Human Recombinant

PRAT4B, Protein canopy homolog 4, CNPY4.

Product # :

PRO-1976

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Description

CNPY4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (22-248 a.a) and having a molecular mass of 28.6kDa. CNPY4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques..

Source

Escherichia Coli.

Formulation

CNPY4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 5mM DTT and 2mM EDTA.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Canopy FGF Signaling Regulator 4 (CNPY4) is a part of the canopy family which owns one saposin B-type domain. CNPY4 takes part in the regulation process of the cell surface expression of TLR4.
Synonyms
PRAT4B, Protein canopy homolog 4, CNPY4.
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 MGSEFGMLKE EDDDTERLPS KCEVCKLLST ELQAELSRTG RSREVLELGQ VLDTGKRKRH VPYSVSETRL EEALENLCER ILDYSVHAER KGSLRYAKGQ SQTMATLKGL VQKGVKVDLG IPLELWDEPS VEVTYLKKQC ETMLEEFEDI VGDWYFHHQE QPLQNFLCEG HVLPAAETAC LQETWTGKEI TDGEEKTEGE EEQEEEEEEE EEEGGDKMTK TGSHPKLDRE DL.

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 Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

Product # :

CYT-222

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Quantity :

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Shipped at Room temp

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Description

Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF Mouse was lyophilized with no additives.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) 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-Thr-Arg.
Background
What is the molecular weight/Mw of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein has a total Mw of 14.28kDa.

What is the source or expression system of GM-CSF MOUSE Protein?
Escherichia Coli.

What is the Purity of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

What is the amino acid sequence of GM-CSF MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

What applications can GM-CSF MOUSE Protein be used in?
GM-CSF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF MOUSE Protein?
The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.
Protein content
GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 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 GM-CSF 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:

Granulocyte Colony Stimulating Factor Recombinant Rhesus Macaque

CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.

Product # :

CYT-1121

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Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.

Purity

Greater than 98.0% 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 NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

More Info

Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part 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
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque 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 Granulocyte Colony Stimulating Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
Background
What is the molecular weight/Mw of GCSF MONKEY Protein?
GCSF MONKEY Protein has a total Mw of 18.9kDa.

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

What is the Purity of GCSF MONKEY Protein?
GCSF MONKEY Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GCSF MONKEY Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

What is the amino acid sequence of GCSF MONKEY Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.

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

What is the endotoxin level for GCSF MONKEY Protein?
The endotoxin level is minimal, GCSF MONKEY 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

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

Product # :

CYT-223

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Description

Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

Purity

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

Biological Activity

The Specific Activity is >5.0×10⁷ IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

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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, INS 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 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.
Background
TNF Alpha Human: An Overview of Its Role and Importance in Immunology
TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.
This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.
Production and Properties
Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.
Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.
Solubility and Usage
The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.
This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.
Storage and Stability
For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.
Biological Role and Implications
TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.
Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.
Mechanism of Action
TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.
Research and Clinical Importance
Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.
Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.
In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.

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:

Cellular Nucleic Acid Binding Protein Human Recombinant

CNBP1, DM2, PROMM, RNF163, ZCCHC22, ZNF9, Cellular nucleic acid-binding protein, CNBP, Zinc finger protein 9.

Product # :

PRO-1371

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Description

CNBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-170 a.a) and having a molecular mass of 21kDa. CNBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CNBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cellular nucleic acid-binding protein (CNBP) is a nucleic-acid binding protein with seven zinc-finger domains, which has a preference for binding single stranded DNA and RNA. CNBP serves in cap-independent translation of ornithine decarboxylase mRNA, and also in sterol-mediated transcriptional regulation. The expansion of A CCTG in CNBP protein’s first intron results in myotonic dystrophy type 2.
Synonyms
CNBP1, DM2, PROMM, RNF163, ZCCHC22, ZNF9, Cellular nucleic acid-binding protein, CNBP, Zinc finger protein 9.
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 MGSMSSNECF KCGRSGHWAR ECPTGGGRGR GMRSRGRGFQ FVSSSLPDIC YRCGESGHLA KDCDLQEDAC YNCGRGGHIA KDCKEPKRER EQCCYNCGKP GHLARDCDHA DEQKCYSCGE FGHIQKDCTK VKCYRCGETG HVAINCSKTS EVNCYRCGES GHLARECTIE ATA.

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 Human Recombinant, CHO

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

Product # :

CYT-329

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in CHO cells is a single, glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18 kDa.G-CSF is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells (CHO).

Formulation

G-CSF was lyophilized from a concentrated (1mg/ml) solution containing 10mM Hydrochloric Acid pH=6.5, 0.4mg tween 20, 100mg mannitol, 160mg L-arginine, 40mg phenylalanine and 4mg methionine.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by ³H-thymidine uptake) is < 0.07 ng/ml, corresponding to a Specific Activity of 1.27 x 10⁸IU/mg.

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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF 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 Granulocyte Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP.
Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 18kDa.

What is the source or expression system of G CSF Protein?
Chinese Hamster Ovary Cells (CHO).

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

What is the Biological Activity of G CSF Protein?
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.07 ng/ml, corresponding to a Specific Activity of 1.27 x 108 IU/mg.

What is the amino acid sequence of G CSF Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP.

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

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

CD30 Ligand Human Recombinant, Sf9

Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

Product # :

CYT-954

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Description

TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
Synonyms
Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.
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
ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH 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:

TRAIL Receptor-4 Human Recombinant

Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.

Product # :

CYT-1045

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Description

TNFRSF10D produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 395 amino acids (56-211a.a.) and having a molecular mass of 73.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10D is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF10D protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a neutralizing assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 10 ng/ml in the presence of 2ng/ml TRAIL.

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Introduction
TRAIL Receptor-4 Human Recombinant or TNFRSF10D, is part of the TNF-receptor superfamily. TNFRSF10D has atruncated cytoplasmic death domai , an extracellular TRAIL-binding domain and a transmembrane domain. The protein can prevent from TRAIL-mediated apoptosis on cells with TRAIL R1 and/or TRAIL R2.
Synonyms
Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.
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
ATIPRQDEVP QQTVAPQQQR RSLKEEECPA GSHRSEYTGA CNPCTEGVDY TIASNNLPSC LLCTVCKSGQ TNKSSCTTTR DTVCQCEKGS FQDKNSPEMC RTCRTGCPRG MVKVSNCTPR SDIKCKNESA ASSTGKTPAA EETVTTILGM LASPYHVEPK SCDKTHTCPP CPAPELLGGP
SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ
QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

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:

GM-CSF Receptor Alpha Sf9 Human Recombinant

Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.

Product # :

CYT-1044

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Description

CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (20-320a.a.) and having a molecular mass of 35.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CSF2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.
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
ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH
Background
GM-CSF Receptor Alpha Human Recombinant: A Glimpse into Its Potential and Implications
Abstract:
Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) receptor alpha, a pivotal component in the GM-CSF signaling pathway, has been the focal point of numerous studies pertaining to hematopoiesis and immune responses. This paper provides an overview of the GM-CSF receptor alpha human recombinant, exploring its characteristics, production techniques, and potential therapeutic applications.
Introduction
GM-CSF, a cytokine responsible for the differentiation and proliferation of white blood cells, functions by binding to its receptor, GM-CSF receptor. The alpha subunit (GM-CSFRα) of this receptor plays a crucial role in ligand binding and is essential for initiating cellular responses. Modern biotechnological advancements have led to the successful production of its human recombinant form, offering new avenues in medical research.
Recombinant GM-CSFRα:
Production and Features Recombinant GM-CSFRα is synthesized using cutting-edge recombinant DNA technologies, predominantly in bacterial or mammalian expression systems. This human recombinant form retains its ability to bind to GM-CSF, maintaining its biological functionality and providing myriad research opportunities.
Therapeutic and Clinical Prospects
1. Autoimmune Diseases: GM-CSF is often overexpressed in various autoimmune disorders. By utilizing recombinant GM-CSFRα as a potential decoy receptor, it's feasible to mitigate the effects of excessive GM-CSF, offering a new therapeutic strategy.
2. Hematopoietic Disorders: Given its integral role in white blood cell development, recombinant GM-CSFRα might hold promise in treatments or as a diagnostic tool for certain hematological conditions.
3. Research Paradigm: Beyond therapeutic applications, the recombinant GM-CSFRα can serve as an invaluable research tool to elucidate the nuances of GM-CSF signaling, aiding in the understanding of immune response mechanisms.
Conclusion:
GM-CSF receptor alpha human recombinant stands at the forefront of exciting research and therapeutic potential. While its full capabilities are yet to be realized, current insights underscore its significance in the realms of immunology and medicine.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 35.9kDa.

What is the source or expression system of CD116 Protein?
Sf9, Baculovirus cells.
What is the Purity of CD116 Protein?
CD116 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 310 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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:

Neuropoietin Mouse Recombinant

Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

Product # :

CYT-1128

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Quantity :

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Shipped at Room temp

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Description

Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

Purity

Greater than 98.0% 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 human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

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Introduction
CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.
Synonyms
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin 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 Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
Background
What is the molecular weight/Mw of CTF2P Protein?
CTF2P Protein has a total Mw of 19.7kDa.

What is the source or expression system of CTF2P Protein?
Escherichia Coli.

What is the Purity of CTF2P Protein?
CTF2P Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF2P Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

What is the amino acid sequence of CTF2P Protein?
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

What applications can CTF2P Protein be used in?
CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF2P Protein?
The endotoxin level is minimal, CTF2P 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:

Cardiotrophin-1 Rat Recombinant

Cardiotrophin-1, CT-1, Ctf1.

Product # :

CYT-199

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.

What is the source or expression system of CTF1 Protein?
Escherichia Coli.

What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.

What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 Canine Recombinant

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

Product # :

CYT-140

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.

Purity

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

Biological Activity

The Specific Activity is >3.3×10⁵ IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

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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, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, 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
VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.

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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