Search results
1000 results found for “hepatocyte growth factor”
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- View Data Sheet
Name :
GHRP1Description:
Growth Hormone Releasing Peptide-1
GHRP-1, GHRP1.
Product # :
HOR-021Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Releasing Peptide-1 Synthetic is a single, non-glycosylated polypeptide chain containing 5 amino acids, having a molecular mass of 955.11 Dalton and a Molecular formula of C51H62N12O7.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
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Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP1 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.
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Synonyms
GHRP-1, GHRP1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Releasing Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP1 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.
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Solubility
It is recommended to reconstitute the lyophilized GHRP1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Ala-His-(D-β-Nal)-Ala-Trp-(D-Phe)-Lys-NH2.
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Background
What is the molecular weight/Mw of GHRP-1 Protein?
GHRP-1 Protein has a total Mw of 0.955kDa.
What is the Purity of GHRP-1 Protein?
GHRP-1 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRP-1 Protein?
The biological functionality of GHRP-1 Protein will be determined in the future.
What is the amino acid sequence of GHRP-1 Protein?
Ala-His-(D-β-Nal)-Ala-Trp-(D-Phe)-Lys-NH2
What applications can GHRP-1 Protein be used in?
GHRP-1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRP-1 Protein?
The endotoxin level is minimal, GHRP-1 Protein was purified using conventional chromatography techniques.
Who supplies GHRP-1 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of GHRP-1?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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.
- View Data Sheet
Name :
CCL14 Human, HisDescription:
HCC-1 (CCL14) Human Recombinant, His Tag
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
Product # :
CHM-253Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HCC-1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids (20-93 a.a.) and having a molecular mass of 10.9kDa. The HCC-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HCC-1 solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.
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Synonyms
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.
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Background
What is the molecular weight/Mw of CCL14 HUMAN, HIS Protein?
CCL14 HUMAN, HIS Protein has a total Mw of 10.9kDa.
What is the source or expression system of CCL14 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL14 HUMAN, HIS Protein?
CCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL14 HUMAN, HIS Protein?
The biological functionality of CCL14 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL14 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.
What applications can CCL14 HUMAN, HIS Protein be used in?
CCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL14 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL14 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL14 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL14 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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.
- View Data Sheet
Name :
HCV E2Description:
Hepatitis C Virus E2 Recombinant
Product # :
HCV-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Hepatitis C Virus E2 Genotype-1 produced in E. coli is a single polypeptide chain containing 226 amino acids (aa 482-671) and having a molecular mass of 25.4kDa (NCBI Accession#NP_671491).HCV E2 is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The HCV E2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
E1 and E2 glycoproteins form a heterodimer which is involved in virus attachment to the host cell, virion internalization via clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, however this binding insufficient for infection, some additional liver specific cofactors may be required. The fusion function may perhaps be conducted by E1. E2 hinders human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively located on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses. These interactions allow seizure of circulating HCV particles by these cells and subsequent diffusion to permissive cells.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSERPY CWHYPPRPCG IVPAKSVCGP VYCFTPSPVV VGTTDRSGAP TYSWGANDTD VFVLNNTRPP LGNWFGCTWM NSTGFTKVCG APPCVIGGVG NNTLLCPTDC FRKHPEATYS RCGSGPWITP RCMVDYPYRL WHYPCTINYT IFKVRMYVGG VEHRLEAACN WTRGERCDLE DRDRSELSPL LLSTTQ.
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.
- View Data Sheet
Name :
MMAB HumanDescription:
Methylmalonic Aciduria Type B Human Recombinant
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
Product # :
ENZ-248Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMAB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (33-250 a.a.) and having a molecular mass of 26.3 kDa. The MMAB is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMAB 1mg/ml protein solution contains 20mM Tris pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MMAB protein catalyzes the last step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12 containing coenzyme for methylmalonyl-CoA mutase(MCM). Decreased MMAB activity leads to the inherited disorder vitamin B12 dependent methylmalonic aciduria linked to the cblB complementation group.
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Synonyms
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MMAB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQSRGPQGVE DGDRPQPSSK TPRIPKIYTK TGDKGFSSTF TGERRPKDDQ VFEAVGTTDE LSSAIGFALE LVTEKGHTFA EELQKIQCTL QDVGSALATP CSSAREAHLK YTTFKAGPIL ELEQWIDKYT SQLPPLTAFI LPSGGKISSA LHFCRAVCRR AERRVVPLVQ MGETDANVAK FLNRLSDYLF TLARYAAMKE GNQEKIYKKN DPSAESEGL.
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.
- View Data Sheet
Name :
NFKBIB HumanDescription:
NF-kappa-B Inhibitor Beta Human Recombinant
NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.
Product # :
PRO-1046Price :
Quantity :
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Shipped with Ice Packs
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Description
NFKBIB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-356 a.a) and having a molecular mass of 40.3kDa (Molecular weight on SDS-PAGE will appear higher).NFKBIB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NFKBIB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NF-kappa-B inhibitor beta (NFKBIB) is a member of the NF-kappa-B inhibitor family, which inhibit NF-kappa-B by complexing with, and trapping it in the cytoplasm. Phosphorylation of serine residues on these proteins by kinases marks them for destruction via the ubiquitination pathway, thus allowing activation of the NF-kappa-B, which translocates to the nucleus to act as a transcription factor.
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Synonyms
NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAGVAC LGKAADADEW CDSGLGSLGP DAAAPGGPGL GAELGPGLSW APLVFGYVTE DGDTALHLAV IHQHEPFLDF LLGFSAGTEY MDLQNDLGQT ALHLAAILGE TSTVEKLYAA GAGLCVAERR GHTALHLACR VGAHACARAL LQPRPRRPRE
APDTYLAQGP DRTPDTNHTP VALYPDSDLE KEEEESEEDW KLQLEAENYE GHTPLHVAVI HKDVEMVRLL RDAGADLDKP EPTCGRSPLH LAVEAQAADV LELLLRAGAN PAARMYGGRT PLGSAMLRPN PILARLLRAH GAPEPEGEDE KSGPCSSSSD SDSGDEGDEY DDIVVHSSRS QTRLPPTPAS KPLPDDPRPV.
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.
- View Data Sheet
Name :
CCDC104 HumanDescription:
Coiled-Coil Domain Containing 104 Human Recombinant
Coiled-Coil Domain Containing 104, Coiled-CoilDomain- Protein104, CCDC104.
Product # :
PRO-1728Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCDC104 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 365 amino acids (1-342 a.a) and having a molecular mass of 41.8kDa.CCDC104 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCDC104 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCDC104 also known as coiled-coil domain-containing protein 104 is a 342 amino acid protein that exists as two alternatively spliced isoforms. CCDC104 undergoes post-translational phosphorylation following DNA damage, most likely by either ATR or ATM. Among the diseases associated with CCDC104 are pancreatic cancer, and pancreatitis.
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Synonyms
Coiled-Coil Domain Containing 104, Coiled-CoilDomain- Protein104, CCDC104.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAEEED EVEWVVESIA GFLRGPDWSI PILDFVEQKC EVFDDEEESK LTYTEIHQEY KELVEKLLEG YLKEIGINED QFQEACTSPL AKTHTSQAIL QPVLAAEDFT IFKAMMVQKN IEMQLQAIRI IQERNGVLPD CLTDGSDVVS DLEHEEMKIL REVLRKSKEE YDQEEERKRK KQLSEAKTEE PTVHSSEAAI MNNSQGDGEH FAHPPSEVKM HFANQSIEPL GRKVERSETS SLPQKDLKIP GLEHASIEGP IANLSVLGTE ELRQREHYLK QKRDKLMSMR KDMRTKQIQN MEQKGKPTGE VEEMTEKPEM TAEEKQTLLK RRLLAEKLKE EVINK
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.
- View Data Sheet
Name :
CDC37 HumanDescription:
Cell Division Cycle 37 Human Recombinant
P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.
Product # :
PRO-464Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDC37 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids and having a molecular mass of 44.4 kDa.
Source
Escherichia Coli.
Formulation
The CDC37 protein solution contains 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CDC37 is an essential protein in Saccharomyces cerevisiae and is a molecular chaperone with precise function in cell signal transduction. CDC37 forms a complex/associates with Hsp90 molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. CDC37 also forms complex with a number of protein kinases such as CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. CDC34 is involved in directing Hsp90 to its target kinases. CDC37 up-regulation is a common early event in some localized human cancers. CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multitargeted therapies. CDC37 plays a role in regulating Hsp90 ATPase activity. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. CDC37 and heat shock protein 90 bind specifically to the kinase domain of LKB1.
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Synonyms
P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV.
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.
- View Data Sheet
Name :
VBP1 HumanDescription:
Von Hippel-Lindau Binding Protein 1 Human Recombinant
Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
Product # :
PRO-1325Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a) and having a molecular mass of 25kDa.VBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VBP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prefoldin subunit 3 (VBP1) is a member of the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein in order to create an intracellular complex. Since VBP1 serves as a chaperone protein, it is assumed to have a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. VBP1 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. VBP1 also binds to nascent polypeptide chain and stimulates folding in an environment in which there are numerous competing pathways for nonnative proteins.
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Synonyms
Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA.
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.
- View Data Sheet
Name :
EEF1G HumanDescription:
Eukaryotic Translation Elongation Factor 1 Gamma Human Recombinant
EF1G, GIG35, Elongation factor 1-gamma, Eukaryotic Translation Elongation Factor 1 Gamma, EEF1G, EF-1-gamma, eEF-1B gamma, PRO1608.
Product # :
PRO-2048Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EEF1G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (1-437) and having a molecular mass of 52.5 kDa.EEF1G is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EEF1G solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Eukaryotic Translation Elongation Factor 1 Gamma (EEF1G) takes part in anchoring the complex to additional cellular components. EEF1G is a multi-protein complex which is in charge of the delivery of aminoacyl-tRNAs to the ribosome. Over expression of EEF1G is linked with pancreatic cancer, due to the role of EEF1G protein in the oncogenic transformation process.
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Synonyms
EF1G, GIG35, Elongation factor 1-gamma, Eukaryotic Translation Elongation Factor 1 Gamma, EEF1G, EF-1-gamma, eEF-1B gamma, PRO1608.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAGTLY TYPENWRAFK ALIAAQYSGA QVRVLSAPPH FHFGQTNRTP EFLRKFPAGK VPAFEGDDGF CVFESNAIAY YVSNEELRGS TPEAAAQVVQ WVSFADSDIV PPASTWVFPT LGIMHHNKQA TENAKEEVRR ILGLLDAYLK TRTFLVGERV TLADITVVCT LLWLYKQVLE PSFRQAFPNT NRWFLTCINQ PQFRAVLGEV KLCEKMAQFD AKKFAETQPK KDTPRKEKGS REEKQKPQAE RKEEKKAAAP APEEEMDECE QALAAEPKAK DPFAHLPKST FVLDEFKRKY SNEDTLSVAL PYFWEHFDKD GWSLWYSEYR FPEELTQTFM SCNLITGMFQ RLDKLRKNAF ASVILFGTNN SSSISGVWVF RGQELAFPLS PDWQVDYESY TWRKLDPGSE ETQTLVREYF SWEGAFQHVG KAFNQGKIFK.
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.
- View Data Sheet
Name :
TFPI2 HumanDescription:
Tissue Factor Pathway Inhibitor 2 Human Recombinant
Tissue Factor Pathway Inhibitor 2, Placental Protein 5, TFPI-2, PP5, Retinal Pigment Epithelium Cell Factor 1, REF1, TFPI2.
Product # :
PRO-860Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TFPI2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 199 amino acids (23-213 a.a.) and having a molecular mass of 22.9kDa (Migrates at 18-40kDa on SDS-PAGE under reducing conditions).TFPI2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TFPI2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TFPI2 takes part in the regulation of plasmin-mediated matrix remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and weakly factor Xa. TFPI2 doesn’t have any influence on thrombin.
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Synonyms
Tissue Factor Pathway Inhibitor 2, Placental Protein 5, TFPI-2, PP5, Retinal Pigment Epithelium Cell Factor 1, REF1, TFPI2.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
DAAQEPTGNN AEICLLPLDY GPCRALLLRY YYDRYTQSCR QFLYGGCEGN ANNFYTWEAC DDACWRIEKV PKVCRLQVSV DDQCEGSTEK YFFNLSSMTC EKFFSGGCHR NRIENRFPDE ATCMGFCAPK KIPSFCYSPK DEGLCSANVT RYYFNPRYRT CDAFTYTGCG GNDNNFVSRE DCKRACAKAL KLEHHHHHH.
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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Name :
EIF1AX HumanDescription:
Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
Product # :
PRO-253Price :
Quantity :
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Shipped with Ice Packs
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Description
EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.
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Synonyms
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI
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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Name :
STAT1 HumanDescription:
Signal Transducer and Activator of Transcription 1 Human Recombinant
Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.
Product # :
PKA-315Price :
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Description
STAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 732 amino acids (1-712 a.a.) and having a molecular mass of 85.2 kDa. The STAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STAT1 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STAT1 is a member of the Signal Transducers and Activators of Transcriptionfamily of transcription factors. STAT1 is involved in upregulating genes due to a signal by either type Ior type IIinterferons. In response to IFN-?stimulation, STAT1 forms homodimers or heterodimers with STAT3that bind to the GAS (Interferon-Gamma Activated Sequence) promoter element; in response to either IFN-? or IFN-?stimulation, STAT1 forms a heterodimer with STAT2that can bind the ISRE (Interferon Stimulated Response Element) promoter element. In either case, binding of the promoter element leads to an increased expression of ISG (Interferon Stimulated Genes).
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Synonyms
Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.
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Physical Appearance
Sterile Filtered clear solution.
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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. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EV.
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.
- View Data Sheet
Name :
Leptin BovineDescription:
Leptin Bovine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-502Price :
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Shipping Method :
Shipped at Room temp
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Description
Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.Citations
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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).
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.
- View Data Sheet
Name :
PEDF HumanDescription:
Pigment Epithelium-Derived Factor Human Recombinant
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Product # :
CYT-580Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.
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Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PEDF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PEDF Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PEDF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
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Background
About PEDF Human
Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
several conditions, including heart disease and cancer.What’s the Function of PEDF Human Recombinant?
PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
only known signaling receptor to be used by a serpin family member.
What’s the Application of PEDF Human Recombinant?This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
by proprietary chromatographic techniques.The main purpose of PEDF human recombinant is for research. It has the potential to
become a potential treatment for different angiogenesis-related diseases, including
various cancers. Moreover, it can become crucial during the recovery from vasculature-
related neurodegenerative illness.Such a discovery could be revolutionary for the world, which is why more research is
needed to determine the effect of this non-inhibitory serpin on the body.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HCV Core 16.8kDaDescription:
Hepatitis C Virus Nucleocapsid (core) 16.8kDa Recombinant
Product # :
HCV-011Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant HCV Core produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 16.8 kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
HCV Core containing PBS, pH-7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Physical Appearance
Sterile filtered colorless solution.
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Stability
HCV Core although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
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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Name :
BMP 7 HumanDescription:
Bone Morphogenetic Protein-7 Human Recombinant
Osteogenic Protein 1, BMP-7.
Product # :
CYT-333Price :
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Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 139 amino acids and having a molecular mass of 15679.97 Dalton. The BMP-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-7 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, BMP-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in 20mM-100mM acetic acid at a concentration of 0.1-0.5mg per ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Thr-Gly-Ser-Lys.
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Background
Bone Morphogenetic Protein-7 Human Recombinant: A Comprehensive Review
Abstract:
Bone Morphogenetic Protein-7 (BMP-7) is a crucial member of the transforming growth factor-beta (TGF-β) superfamily with diverse roles in development, tissue repair, and regeneration.
This research paper provides a comprehensive review of BMP-7 Human Recombinant, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the therapeutic potential of BMP-7 modulation.
Introduction:
BMP-7 is a multifunctional growth factor that plays a significant role in skeletal development and tissue homeostasis. This paper aims to provide an extensive review of BMP-7 Human Recombinant, highlighting its importance in various biological processes and its potential therapeutic applications.
Structure and Function of BMP-7:
BMP-7 is a disulfide-linked homodimeric protein composed of two subunits. It binds to specific cell surface receptors, activating downstream signaling pathways, including the Smad pathway and non-Smad signaling cascades. These pathways regulate cellular processes such as proliferation, differentiation, and apoptosis.
Skeletal Development and Regeneration:
BMP-7 is a key regulator of bone formation and remodeling. It promotes osteoblast differentiation and bone mineralization, contributing to skeletal development and repair. BMP-7 also plays a role in cartilage formation and chondrogenesis.
Tissue Repair and Regeneration:
Beyond its skeletal functions, BMP-7 is involved in tissue repair and regeneration in various organs, including the kidney, liver, and heart. It promotes the regeneration of damaged tissues by stimulating cell proliferation, angiogenesis, and extracellular matrix remodeling.
Therapeutic Potential:
Due to its regenerative and reparative properties, BMP-7 has attracted significant attention as a potential therapeutic agent. It has been investigated for its applications in bone regeneration, cartilage repair, and the treatment of kidney and liver diseases. Clinical trials exploring the therapeutic efficacy of BMP-7 are ongoing.
Challenges and Future Perspectives:
Despite the promising therapeutic potential of BMP-7, challenges remain, including optimizing its delivery systems, understanding its dosage and duration of treatment, and managing potential side effects. Future research should focus on unraveling the intricate mechanisms of BMP-7 signaling, developing targeted therapies, and enhancing its clinical applications.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 15kDa.
What is the source or expression system of BMP7 Protein?
Escherichia Coli.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.
What is the amino acid sequence of BMP7 Protein?
BMP7 Protein is composed from 139 amino acids.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CNTFR HumanDescription:
Ciliary Neurotrophic Factor Receptor Human Recombinant
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
Product # :
CYT-883Price :
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Shipping Method :
Shipped with Ice Packs
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- sds-page
- Citations
Description
CNTFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (23-342 a.a) and having a molecular mass of 38.1kDa. CNTFR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
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Synonyms
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
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Physical Appearance
Sterile Filtered colorless clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.
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Background
Unveiling the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Insights and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) holds a crucial role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper discusses the significance of Human Recombinant CNTFR, its production methods, and its potential applications in neurobiology and therapeutic interventions. The review sheds light on the pivotal role of CNTFR in neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, plays a pivotal role in transmitting CNTF-mediated signals to the cell. The availability of Human Recombinant CNTFR allows researchers to investigate its role in neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's involvement in modulating neuronal health and promoting regeneration makes it an essential component in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and initiate downstream signaling pathways. Activation of intracellular signaling cascades, such as JAK/STAT and MAPK, contributes to the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is produced through gene expression in suitable host cells, often employing bacterial or mammalian systems. Ensuring proper folding and post-translational modifications is essential to maintain its functionality and binding affinity for CNTF.
Therapeutic Applications:
The availability of Human Recombinant CNTFR offers potential therapeutic applications in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-mediated signaling presents opportunities to enhance neuronal survival and regeneration, ultimately improving patient outcomes.
Challenges and Future Directions:
While promising, challenges include optimizing the interaction between CNTFR and CNTF, ensuring efficient delivery to target tissues, and understanding potential off-target effects. Ongoing research is essential to unravel the complete mechanisms of CNTFR-mediated signaling and its implications for therapy.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor serves as a crucial tool in advancing our understanding of neuroprotection and regeneration. Its potential to modulate CNTF-mediated effects opens avenues for innovative therapeutic strategies targeting neurodegenerative disorders, exemplifying the intersection of molecular biology and clinical application.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 38.1kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography tech
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HDAC2 HumanDescription:
Histone Deacetylase 2 Human Recombinant
Histone deacetylase 2, YAF1, HD2, YY1-associated factor 1, transcriptional regulator homolog RPD3, RPD3, EC 3.5.1.98.
Product # :
ENZ-157Price :
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Description
HDAC2 Human Recombinant produced in Hi-5 Cell is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-488) and having a molecular mass of 56.4 kDa.The HDAC2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Hi-5 Cell.
Formulation
The HDAC2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl, 0.1mM PMSF and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures. -
Synonyms
Histone deacetylase 2, YAF1, HD2, YY1-associated factor 1, transcriptional regulator homolog RPD3, RPD3, EC 3.5.1.98.
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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.
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Amino Acid Sequence
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDTKGT KSEQLSNPSR HHHHHH
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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Name :
KLF4 HumanDescription:
Kruppel-Like Factor 4 Human Recombinant
Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.
Product # :
PRO-891Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLF4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 545 amino acids (11-395) and having a molecular mass of 58.1 kDa.The KLF4 is fused to a 159 amino acid His-CaM Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KLF4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.
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Synonyms
Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MAHHHHHHMA DQLTEEQIAE FKEAFSLFDK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGYIS AAELRHVMTN LGEKLTDEEV DEMIREADID GDGQVNYEEF VQMMTAKGSM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV PPLHYQELMP PGSCMPEEPK PKRGRRSWPR KRTAT
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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Name :
MAX HumanDescription:
MYC Associated Factor X Human Recombinant
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
Product # :
PRO-811Price :
Quantity :
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Description
MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
MAX Human solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.
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Synonyms
bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FCGR2A Human, HEKDescription:
CD32a Human Recombinant, HEK
CD32, CD32A, CDw32, FcGR, IGFR2, MGC23887, MGC30032, Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a, Fc-gamma-RIIa, FcRII-a, FCG2, FCGR2A1.
Product # :
PRO-2775Price :
Quantity :
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Shipped with Ice Packs
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Description
FCGR2A Human Recombinant is a single, glycosylated, polypeptide chain (30-218 a.a) containing a total of 195 amino acids, having a molecular mass of 21.6kDa. FCGR2A is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
FCGR2A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤5 ug/ml. and is measured by its binding ability in a functional ELISA with Human IgG1 Fc (CAT# pro-2763).
Citations
More Info
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Synonyms
CD32, CD32A, CDw32, FcGR, IGFR2, MGC23887, MGC30032, Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a, Fc-gamma-RIIa, FcRII-a, FCG2, FCGR2A1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
SADSQAAAPP KAVLKLEPPW INVLQEDSVT LTCQGARSPE SDSIQWFHNG NLIPTHTQPS YRFKANNNDS GEYTCQTGQT SLSDPVHLTV LSEWLVLQTP HLEFQEGETI MLRCHSWKDK PLVKVTFFQN GKSQKFSHLD PTFSIPQANH SHSGDYHCTG NIGYTLFSSK PVTITVQVPS MGSSSPMGIH HHHHH.
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Background
The immune system is a complex network of cells and molecules that play a crucial role in protecting the body against pathogens and maintaining homeostasis. Fc gamma receptors (FcγRs) are a family of cell surface receptors that mediate the effector functions of antibodies, particularly immunoglobulin G (IgG). Among these receptors, FCGR2A, also known as CD32a, is a prominent member expressed on the surface of various immune cells. This research aims to investigate the structure, function, and implications of FCGR2A protein in immune responses, with a focus on its relevance to human health and therapeutic applications.
Structure and Expression of FCGR2A:
FCGR2A is a transmembrane glycoprotein composed of two extracellular immunoglobulin-like domains, a transmembrane domain, and a cytoplasmic tail. It is primarily expressed on immune cells such as macrophages, monocytes, and dendritic cells. The unique structure of FCGR2A allows it to bind to the Fc portion of IgG antibodies, initiating immune effector functions.
Role of FCGR2A in Immune Responses:
FCGR2A plays a crucial role in modulating immune responses through its involvement in antibody-dependent cellular cytotoxicity (ADCC) and phagocytosis. Upon binding to IgG antibodies, FCGR2A triggers intracellular signaling cascades that activate immune effector cells, leading to the elimination of antibody-bound pathogens or targeted cells. Furthermore, FCGR2A is involved in immune complex clearance, regulation of cytokine production, and modulation of cellular activation, thus contributing to the overall immune response.
Implications of FCGR2A in Human Health:
The dysregulation of FCGR2A has been implicated in various immune-related diseases. Genetic variations in FCGR2A have been associated with increased susceptibility to autoimmune disorders, such as systemic lupus erythematosus and rheumatoid arthritis. Altered FCGR2A expression or function has also been observed in infectious diseases, including HIV and malaria, affecting disease progression and immune control. Understanding the role of FCGR2A in these conditions is crucial for developing targeted therapeutic strategies.
Therapeutic Potential of FCGR2A:
The unique properties of FCGR2A make it an attractive target for therapeutic interventions. Modulating FCGR2A activity and function can potentially enhance immune responses against pathogens or tumor cells. For example, monoclonal antibodies that target FCGR2A have shown promising results in cancer immunotherapy by promoting ADCC and phagocytosis of tumor cells. Furthermore, strategies aimed at selectively activating or inhibiting FCGR2A signaling could lead to the development of novel immunotherapeutic approaches.
Challenges and Future Perspectives:
While the study of FCGR2A holds great promise, several challenges need to be addressed. Further research is required to unravel the intricate interplay between FCGR2A and other immune receptors and signaling molecules. Additionally, the development of therapeutic agents that selectively target FCGR2A without compromising normal immune functions remains a challenge.
Conclusion:
The investigation of FCGR2A protein provides insights into its pivotal role in immune responses and its implications for human health and therapeutics. Understanding the structure, function, and dysregulation of FCGR2A in immune-related diseases opens avenues for the development of targeted therapies. Continued research on FCGR2A and its interactions within the immune system will contribute to advancements in immunotherapy and personalized medicine.
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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Name :
HEXA Human, Sf9Description:
Hexosaminidase A Human Recombinant, SF9
Hexosaminidase A (Alpha Polypeptide), N-Acetyl-Beta-Glucosaminidase Subunit Alpha, Beta-N-Acetylhexosaminidase Subunit Alpha, Hexosaminidase Subunit A, EC 3.2.1.52, TSD, Beta-Hexosaminidase Subunit Alpha, GM2 Gangliosidosis, Tay Sachs Disease, EC 3.2.1, Beta-hexosaminidase subunit alpha, Beta-N-acetylhexosaminidase subunit alpha, Hexosaminidase subunit A, N-acetyl-beta-glucosaminidase subunit alpha.
Product # :
ENZ-881Price :
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Description
HEXA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 513 amino acids (23-529a.a.) and having a molecular mass of 59.2kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). HEXA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HEXA protein solution (0. 5mg/ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HEXA is the alpha subunit of the lysosomal enzyme beta-hexosaminidase which, combined with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules having N-acetyl hexosamines terminus. The two subunits composing Beta-hexosaminidase, alpha and beta, belong to the glycosyl hydrolases family and are encoded by distinct genes. Alpha subunit gene mutations can cause Tay-Sachs disease (GM2-gangliosidosis type I).
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Synonyms
Hexosaminidase A (Alpha Polypeptide), N-Acetyl-Beta-Glucosaminidase Subunit Alpha, Beta-N-Acetylhexosaminidase Subunit Alpha, Hexosaminidase Subunit A, EC 3.2.1.52, TSD, Beta-Hexosaminidase Subunit Alpha, GM2 Gangliosidosis, Tay Sachs Disease, EC 3.2.1, Beta-hexosaminidase subunit alpha, Beta-N-acetylhexosaminidase subunit alpha, Hexosaminidase subunit A, N-acetyl-beta-glucosaminidase subunit alpha.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
LWPWPQNFQT SDQRYVLYPN NFQFQYDVSS AAQPGCSVLD EAFQRYRDLL FGSGSWPRPY LTGKRHTLEK NVLVVSVVTP GCNQLPTLES VENYTLTIND DQCLLLSETV WGALRGLETF SQLVWKSAEG TFFINKTEIE DFPRFPHRGL LLDTSRHYLP LSSILDTLDV MAYNKLNVFH WHLVDDPSFP YESFTFPELM RKGSYNPVTH IYTAQDVKEV IEYARLRGIR VLAEFDTPGH TLSWGPGIPG LLTPCYSGSE PSGTFGPVNP SLNNTYEFMS TFFLEVSSVF PDFYLHLGGD EVDFTCWKSN PEIQDFMRKK GFGEDFKQLE SFYIQTLLDI VSSYGKGYVV WQEVFDNKVK IQPDTIIQVW REDIPVNYMK ELELVTKAGF RALLSAPWYL NRISYGPDWK DFYIVEPLAF EGTPEQKALV IGGEACMWGE YVDNTNLVPR LWPRAGAVAE RLWSNKLTSD LTFAYERLSH FRCELLRRGV QAQPLNVGFC EQEFEQTHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
INSR HumanDescription:
Insulin Receptor Human Recombinant
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
Product # :
CYT-777Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 28-944 of the short isoform- HIR-A, Uniprot accession # P06213-2 which includes the whole subunit alpha and extracellular domain of subunit beta) containing a total of 927 amino acids, having a molecular mass of 105.9kDa (calculated), though it migrates at approximately 160kDa on SDS PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.The Human INSR is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
INSR was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Insulin Receptor (INSR) is a receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Once the precursor signal peptide is removed, the insulin receptor precursor is post-translationally cleaved into 2 chains (alpha and beta) which are covalently linked. Insulin binding initiates phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins function as docking proteins for other signaling proteins which contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2.
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Synonyms
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. INSR is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ASHLYPGEVC PGMDIRNNLT RLHELENCSV IEGHLQILLM FKTRPEDFRD LSFPKLIMIT DYLLLFRVYG LESLKDLFPN LTVIRGSRLF FNYALVIFEM VHLKELGLYN LMNITRGSVR IEKNNELCYL ATIDWSRILD SVEDNYIVLN KDDNEECGDI CPGTAKGKTN CPATVINGQF VERCWTHSHC QKVCPTICKS HGCTAEGLCC HSECLGNCSQ PDDPTKCVAC RNFYLDGRCV ETCPPPYYHF QDWRCVNFSF CQDLHHKCKN SRRQGCHQYV IHNNKCIPEC PSGYTMNSSN LLCTPCLGPC PKVCHLLEGE KTIDSVTSAQ ELRGCTVING SLIINIRGGN NLAAELEANL GLIEEISGYL KIRRSYALVS LSFFRKLRLI RGETLEIGNY SFYALDNQNL RQLWDWSKHN LTITQGKLFF HYNPKLCLSE IHKMEEVSGT KGRQERNDIA LKTNGDQASC ENELLKFSYI RTSFDKILLR WEPYWPPDFR DLLGFMLFYK EAPYQNVTEF DGQDACGSNS WTVVDIDPPL RSNDPKSQNH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVFWERQAED SELFELDYCL KGLKLPSRTW SPPFESEDSQ KHNQSEYEDS AGECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP SRKRRSLGDV GNVTVAVPTV AAFPNTSSTS VPTSPEEHRP FEKVVNKESL VISGLRHFTG YRIELQACNQ DTPEERCSVA AYVSARTMPE AKADDIVGPV THEIFENNVV HLMWQEPKEP NGLIVLYEVS YRRYGDEELH LCVSRKHFAL ERGCRLRGLS PGNYSVRIRA TSLAGNGSWT EPTYFYVTDY LDVPSNIAKK LHHHHHH.
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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Name :
MIF AntibodyDescription:
Macrophage Migration Inhibitory Factor, Mouse Anti Human
Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.
Product # :
ANT-311Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.
Citations
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.
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Immunogen
Anti-human MIF mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human MIF amino acids 1-114 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P4E4AT.
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Applications
MIF antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
MIF antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.