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Name :
CXCL14 HumanDescription:
BRAK (CXCL14) Human Recombinant
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Product # :
CHM-001Price :
Quantity :
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Shipped at Room temp
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Description
CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized after extensive dialysis against 20mM Tris-HCl, pH 8.5 and 1M NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL14 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.
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Background
What is the molecular weight/Mw of CXCL14 HUMAN Protein?
CXCL14 HUMAN Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL14 HUMAN Protein?
CXCL14 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 HUMAN Protein?
The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.
What applications can CXCL14 HUMAN Protein be used in?
CXCL14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 HUMAN Protein?
The endotoxin level is minimal, CXCL14 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FABP1 MouseDescription:
Fatty Acid Binding Protein-1 Mouse Recombinant
Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.
Product # :
PRO-1121Price :
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Description
Fatty Acid Binding Protein-1 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The FABP1 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:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.
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Synonyms
Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FABP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized FABP1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI.
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 :
FBP1 Human, ActiveDescription:
Fructose-1,6-Bisphosphatase 1, BioActive Human Recombinant
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
Product # :
ENZ-1145Price :
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Description
FBP1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338) and having a molecular mass of 39.0 kDa.FBP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FBP1 protein solution (1mg/ml) contains 1mM DTT, 10% glycerol and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 7,000pmol/min/ug, and is determined by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. 1 unit oxidizes 1.0pmole of fructose 1,6 diphosphate to fructose 6- phosphate and inorganic phosphate per minute at pH 9.5 at 37˚C.
More Info
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Introduction
FBP1 or Fructose-1, 6-bisphosphatase 1 is an enzyme, catalyzing the formation of fructose 6-phosphate & inorganic phosphate from fructose 1, 6-bisphosphate. FBP1 is part of the gluconeogenesis regulatory enzymes. Mutations in the enzyme gene can result in metabolic acidosis & hypoglycemia.
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Synonyms
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
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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 MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ
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 :
CALB1 RatDescription:
Calbindin-1 Rat Recombinant
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, Spot 35 protein, Calb1, CaBP28K, MGC93326.
Product # :
PRO-400Price :
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Description
Recombinant Rat Calbindin-1 produced in E.Coli.The Rat CALB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution (1mg/ml) containing 50mM NaHCO3.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Calbindins are Ca-binding proteins belonging to the troponin C superfamily. CALB28K/Calbindin1/CALB1 (D28K/Spot35 protein or cholecalcin, rat 261 aa; mouse 261 aa; human 261-aa, chromosome 8q21.3-q22.1) was originally described as 27-kDA induced by vitamin D in the duodenum of chicken. In mammals, it is expressed in the kidney, pancreatic islets, and brain. In brain, its synthesis is independent of vitamin D. CABP28K contains 4 active and 2 inactive EF-hand Ca-binding domains. The gene for CABP28K is clustered in the same region as carbonic anhydrase. The neurons in the brains of patients with Huntington disease are CAB28K depleted. There are two types of CaBPs: the "trigger"- and the "buffer"-CaBPs. The conformation of "trigger" type CaBPs changes upon Ca2+ binding and exposes regions on protein that interact with target molecules, thus altering their activity. The buffer-type CABP are thought to control the intracellular calcium concentration. Calbindin D-28K is found predominantly in subpopulations of central and peripheral nervous system neurons, and in certain epithelial cells involved in Ca2+ transport such as distal tubular cells and cortical collecting tubules of the kidney, and in enteric neuroendocrine cells.
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Synonyms
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, Spot 35 protein, Calb1, CaBP28K, MGC93326.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CABP28K although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CABP28K 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 CABP28K in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
CABP28K can be used for immunoblots, absorption experiments in immunohistochemistry, radioimmunoassay and intracellular injection.
For adsorption we suggest the following procedureA- Dilute 1 µl of the monoclonal antibody against calbindin D-28k in 5 ml of the usual buffer for immunohistochemistry (final dilution 1:5'000).
B- Add 1 µg of the recombinant protein to 1 ml of the diluted antibody solution and mix well.
C- Incubate for at least 6 hours in the cold.
D- Apply to tissue-sections and incubate for 3 days.
E- Complete the immunohistochemical reaction as usual (biotinylated second antibody, ABC-complex, DAB).
As a result, the immunostaining should be strongly reduced or even completely prevented.
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 :
PGP Human, ActiveDescription:
Phosphoglycolate Phosphatase Human Recombinant, Active
Glycerol-3-phosphate phosphatase, G3PP, Aspartate-based ubiquitous Mg(2+)-dependent phosphatase, AUM, Phosphoglycolate phosphatase, PGP.
Product # :
ENZ-1044Price :
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Description
PGP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-321a.a) and having a molecular mass of 36.5kDa.PGP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PGP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT..
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
More Info
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Introduction
Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.
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Synonyms
Glycerol-3-phosphate phosphatase, G3PP, Aspartate-based ubiquitous Mg(2+)-dependent phosphatase, AUM, Phosphoglycolate phosphatase, PGP.
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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 MGSHMAAAEA GGDDARCVRL SAERAQALLA DVDTLLFDCD GVLWRGETAV PGAPEALRAL RARGKRLGFI TNNSSKTRAA YAEKLRRLGF GGPAGPGASL EVFGTAYCTA LYLRQRLAGA PAPKAYVLGS PALAAELEAV GVASVGVGPE PLQGEGPGDW LHAPLEPDVR AVVVGFDPHF SYMKLTKALR YLQQPGCLLV GTNMDNRLPL ENGRFIAGTG CLVRAVEMAA QRQADIIGKP SRFIFDCVSQ EYGINPERTV MVGDRLDTDI LLGATCGLKT ILTLTGVSTL GDVKNNQESD CVSKKKMVPD FYVDSIADLL PALQG.
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 :
PI3 Human, Sf9Description:
Peptidase Inhibitor 3 Human Recombinant, Sf9
Elafin, ESI, SKALP, WAP3, WFDC14.
Product # :
PRO-2653Price :
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Description
PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.
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Synonyms
Elafin, ESI, SKALP, WAP3, WFDC14.
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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
AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH 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.
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Name :
TIGIT HumanDescription:
T-Cell Immunoreceptor With Ig And ITIM Domains Human Recombinant
VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.
Product # :
PRO-2498Price :
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Description
TIGIT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 359 amino acids (22-141a.a.) and having a molecular mass of 40.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TIGIT is expressed with a 239 amino acid hlgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TIGIT protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
T cell immunoreceptor with Ig and ITIM domains or TIGIT, is an immune receptor located on part of T cells and Natural Killer Cells(NK). TIGIT is also known as Vstm3 and WUCAM. The receptor can bind with high affinity to dendritic cells(DCs), CD155(PVR) on macrophages, etc., and it can bind with lower affinity to CD112(PVRL2). TIGIT can inhibit the cytotoxicity of Natural Killer Cells through its ITIM domain via antibodies against the interaction with PVR and the activity is directed. It has been show on research that TIGIT-Fc fusion molecule can have interaction with PVR on dendritic cells and elevate its IL-10 secretion level or lower the secretion on IL-12 under the stimulation of LPS, moreover, it can inhibit the activation of T cell in vivo.
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Synonyms
VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.
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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
MMTGTIETTG NISAEKGGSI ILQCHLSSTT AQVTQVNWEQ QDQLLAICNA DLGWHISPSF KDRVAPGPGL GLTLQSLTVN DTGEYFCIYH TYPDGTYTGR IFLEVLESSV AEHGARFQIP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.
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 :
TPA (311-562) HumanDescription:
Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
Product # :
ENZ-1023Price :
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Description
TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 261 amino acids (311-562 a.a.) and having a molecular mass of 29.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).TPA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TPA protein solution (0.5mg/ml) contains 50mM MES (pH 5.0), 5mM CaCl2, 1mM DTT, 0.5M NaCl and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. -
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
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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
ADPIKGGLFA DIASHPWQAA IFAKHRRSPG ERFLCGGILI SSCWILSAAH CFQERFPPHH LTVILGRTYR VVPGEEEQKF EVEKYIVHKE FDDDTYDNDI ALLQLKSDSS RCAQESSVVR TVCLPPADLQ LPDWTECELS GYGKHEALSP FYSERLKEAH VRLYPSSRCT SQHLLNRTVT DNMLCAGDTR SGGPQANLHD ACQGDSGGPL VCLNDGRMTL VGIISWGLGC GQKDVPGVYT KVTNYLDWIR DNMRPHHHHH 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.
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Name :
PPP1R11 HumanDescription:
Protein Phosphatase 1, Regulatory Subunit 11 Human Recombinant
HCG-V, HCGV, IPP3, TCTE5, TCTEX5, Protein phosphatase 1 regulatory subunit 11, Hemochromatosis candidate gene V protein, PPP1R11.
Product # :
PRO-1526Price :
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Description
PPP1R11 Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (1-126) and having a molecular mass of 16.3 kDa. PPP1R11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPP1R11 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Protein phosphatase 1 regulatory subunit 11 (PPP1R11) is located within the major histocompatibility complex class I region on chromosome 6 and is expressed in a variety of both adult and embryonic tissues. PPP1R11 acts as an inhibitor of PP1 (protein phosphatase 1), particularly showing a sensitivity toward the metal-independent and metal-dependent forms of PP1. Deletion of a portion of the q arm of chromosome 6 is related with early onset intestinal cancer, proposing the presence of a cancer vulnerability locus.
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Synonyms
HCG-V, HCGV, IPP3, TCTE5, TCTEX5, Protein phosphatase 1 regulatory subunit 11, Hemochromatosis candidate gene V protein, PPP1R11.
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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 MGSMAEAGAG LSETVTETTV TVTTEPENRS LTIKLRKRKP EKKVEWTSDT VDNEHMGRRS SKCCCIYEKP RAFGESSTES DEEEEEGCGH THCVRGHRKG RRRATLGPTP TTPPQPPDPS QPPPGPMQH.
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 :
LGALS3 MouseDescription:
Galectin-3 Mouse Recombinant
CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2, Galectin-3, Lectin, galactose binding, soluble 3, Lectin, galactose binding, soluble 3, isoform CRA_a, Lectin, galactose binding, soluble 3, isoform CRA_d, Lgals3.
Product # :
CYT-188Price :
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- sds-page
Description
LGALS3 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 287 amino acids (1-264) and having a molecular mass of 29.8 kDa. LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The LGALS3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 1mM DTT and 2mM EDTA.
Purity
Greater than 95% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2, Galectin-3, Lectin, galactose binding, soluble 3, Lectin, galactose binding, soluble 3, isoform CRA_a, Lectin, galactose binding, soluble 3, isoform CRA_d, Lgals3.
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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 MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
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Background
What is the molecular weight/Mw of LGALS3 Protein?
LGALS3 Protein has a total Mw of 29.8kDa.
What is the source or expression system of LGALS3 Protein?
Escherichia Coli.
What is the Purity of LGALS3 Protein?
LGALS3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 Protein?
The biological functionality of LGALS3 Protein will be determined in the future.
What is the amino acid sequence of LGALS3 Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
What applications can LGALS3 Protein be used in?
LGALS3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 Protein?
The endotoxin level is minimal, LGALS3 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 :
CFLAR HumanDescription:
CASP8 and FADD-Like Apoptosis Regulator Human Recombinant
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
Product # :
PRO-920Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CFLAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (1-480) and having a molecular mass of 55.3 kDa.The CFLAR is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CFLAR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
The precise role of CFLAR is not yet revealed but it seems it is vital in apoptosis regulation downstream of all identified death receptors.
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Synonyms
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
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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
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKMFFIQNY VVSEGQLENS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLILSYT.
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 :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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
MGSSHHHHHH SSGLVPRGSH MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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 :
UCHL1 MouseDescription:
Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Product # :
PRO-2235Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223a.a) and having a molecular mass of 27.2kDa. UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UCHL1 protein solution (1mg/ml) containing Phosphate buffered saline, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.
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Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
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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
MGSSHHHHHH SSGLVPRGSH MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPAC ALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQF LSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGA SSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.
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 :
UCHL1 Mouse, ActiveDescription:
Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant, Active
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Product # :
PRO-2424Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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- biological activity
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Description
UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 27.2kDa. UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UCHL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 70 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.
More Info
-
Introduction
Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.
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Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
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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
MGSSHHHHHH SSGLVPRGSH MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPAC ALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQF LSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGA SSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.
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 :
COMP Human, HEKDescription:
Cartilage Oligomeric Matrix Protein Human Recombinant, HEK
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5.
Product # :
PRO-132Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
COMP HEK Protein is a 82.4 kDa protein containing 750 aa fused to a 13 aa N-Terminal FLAG-tag.
Source
HEK293
Formulation
COMP HEK Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5
More Info
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Introduction
COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. Intact COMP is pentameric, with five equal subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. COMP molecules are vital for conserving the properties and integrity of collagen network. Moreover COMP has a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. Mutations of the COMP gene cause Pseudoachondroplasia and some forms of multiple epiphyseal dysplasia which implicates that it is vital that COMP develops and functions normally. It is a well-known fact that serum levels of COMP offer essential data about metabolic changes taking place in the cartil
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Synonyms
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5.
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Stability
Store lyophilized COMP HEK Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted COMP HEK can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGQGQSPLG SDLGPQMLRE LQETNAALQD VRELLRQQVR EITFLKNTVM ECDACGMQQS VRTGLPSVRP LLHCAPGFCF PGVACIQTES GARCGPCPAG FTGNGSHCTD VNECNAHPCF PRVRCINTSP GFRCEACPPG YSGPTHQGVG LAFAKANKQV CTDINECETG QHNCVPNSVC INTRGSFQCG PCQPGFVGDQ ASGCQRRAQR FCPDGSPSEC HEHADCVLER DGSRSCVCAV GWAGNGILCG RDTDLDGFPD EKLRCPERQC RKDNCVTVPN SGQEDVDRDG IGDACDPDAD GDGVPNEKDN CPLVRNPDQR NTDEDKWGDA CDNCRSQKND DQKDTDQDGR GDACDDDIDG DRIRNQADNC PRVPNSDQKD SDGDGIGDAC DNCPQKSNPD QADVDHDFVG DACDSDQDQD GDGHQDSRDN CPTVPNSAQE DSDHDGQGDA CDDDDDNDGV PDSRDNCRLV PNPGQEDADR DGVGDVCQDD FDADKVVDKI DVCPENAEVT LTDFRAFQTV VLDPEGDAQI DPNWVVLNQG REIVQTMNSD PGLAVGYTAF NGVDFEGTFH VNTVTDDDYA GFIFGYQDSS SFYVVMWKQM EQTYWQANPF RAVAEPGIQL KAVKSSTGPG EQLRNALWHT GDTESQVRLL WKDPRNVGWK DKKSYRWFLQ HRPQVGYIRV RFYEGPELVA DSNVVLDTTM RGGRLGVFCF SQENIIWANL RYRCNDTIPE DYETHQLRQA
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 :
HAND1 HumanDescription:
Heart and Neural Crest Derivatives Expressed 1 Human Recombinant
Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.
Product # :
PRO-1231Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HAND1 Human Recombinant produced in E. coli is a single polypeptide chain containing 238 amino acids (1-215) and having a molecular mass of 26.0 kDa.HAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HAND1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
HAND1 is a member of the basic helix-loop-helix family of transcription factors. HAND1 is one of two HAND proteins, two closely related family members that are irregularly expressed in the emerging ventricular chambers and have a key part in cardiac morphogenesis. Operating in a complementary manner, they work in the development of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. Furthermore, HAND1 is obligatory for early trophoblast differentiation.
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Synonyms
Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.
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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
MGSSHHHHHH SSGLVPRGSH MGSMNLVGSY AHHHHHHHPH PAHPMLHEPF LFGPASRCHQ ERPYFQSWLL SPADAAPDFP AGGPPPAAAA AATAYGPDAR PGQSPGRLEA LGGRLGRRKG SGPKKERRRT ESINSAFAEL RECIPNVPAD TKLSKIKTLR LATSYIAYLM DVLAKDAQSG DPEAFKAELK KADGGRESKR KRELQQHEGF PPALGPVEKR IKGRTGWPQQ VWALELNQ
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 :
MCL1 HumanDescription:
Myeloid Cell Leukemia Sequence 1 Human Recombinant
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
Product # :
PRO-1202Price :
Quantity :
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Shipped with Ice Packs
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Description
MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.
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Synonyms
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
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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
MGSSHHHHHH SSGLVPRGSH MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.
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 :
REN HumanDescription:
Renin Human Recombinant
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
Product # :
PRO-1529Price :
Quantity :
Shipping Method :
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Description
REN Human Recombinant produced in E. coli is a single polypeptide chain containing 365 amino acids (67-406) and having a molecular mass of 39.9kDa. REN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The REN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
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Synonyms
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLTLGN TTSSVILTNY MDTQYYGEIG IGTPPQTFKV VFDTGSSNVW VPSSKCSRLY TACVYHKLFD ASDSSSYKHN GTELTLRYST GTVSGFLSQD IITVGGITVT QMFGEVTEMP ALPFMLAEFD GVVGMGFIEQ AIGRVTPIFD NIISQGVLKE DVFSFYYNRD SENSQSLGGQ IVLGGSDPQH YEGNFHYINL IKTGVWQIQM KGVSVGSSTL LCEDGCLALV DTGASYISGS TSSIEKLMEA LGAKKRLFDY VVKCNEGPTL PDISFHLGGK EYTLTSADYV FQESYSSKKL CTLAIHAMDI PPPTGPTWAL GATFIRKFYT EFDRRNNRIG FALAR.
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 :
RNF181 HumanDescription:
Ring Finger Protein 181 Human Recombinant
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
Product # :
PRO-1218Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).
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Synonyms
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
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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
MGSSHHHHHH SSGLVPRGSH MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.
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 :
SNAPIN HumanDescription:
SNAP Associated Protein Human Recombinant
SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.
Product # :
PRO-663Price :
Quantity :
Shipping Method :
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Description
SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
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Introduction
SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
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Synonyms
SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.
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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 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.
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 N82K Human, PEGDescription:
Leptin N82K Human Recombinant, Pegylated
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1107Price :
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Shipping Method :
Shipped at Room temp
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Description
Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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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 Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, 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.
- View Data Sheet
Name :
BNP HumanDescription:
B-type Natriuretic Peptide Human
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-369Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
B-type Natriuretic Peptide Human is a polypeptide chain containing 32 amino acids and having a molecular mass of 3464 Dalton. The molecular formula is:C143H244N50O42S4.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by RP-HPLC.
More Info
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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B-type Natriuretic Peptide 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 B-type Natriuretic Peptide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
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Background
What is the molecular weight / Mw of BNP Human?
BNP Human has a total Mw of 3.4kDa.
What is the source or expression system of BNP Human?
Synthetic.
What is the Purity of BNP Human?
BNP Human is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP Human?
The biological functionality of BNP Human will be determined in the future.
What is the amino acid sequence of BNP Human?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
What applications can BNP Human Protein be used in?
BNP Human can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP Human?
The endotoxin level is minimal, BNP Human 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 :
GAP43 HumanDescription:
Growth Associated Protein 43 Human Recombinant
Growth associated protein 43, Axonal membrane protein GAP-43, Neural phosphoprotein B-50, calmodulin-binding protein P-57, nerve growth-related peptide GAP43, neuromodulin, protein F1, pp46, B-50.
Product # :
PRO-1126Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GAP43 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (1-238) and having a molecular mass of 27.3kDa (Molecular size on SDS-PAGE will appear higher).GAP43 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GAP43 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GAP43 is a phosphoprotein of the presynaptic membrane that takes part in synaptic reorganization and neural development. GAP43 is found in large quantities in neuronal growth cones all through the development and axonal regeneration. Additionally, GAP43 is involved in specific regions of the normal adult nervous system and has a vital part in the conservation mechanism of long-term potentiation (LTP).
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Synonyms
Growth associated protein 43, Axonal membrane protein GAP-43, Neural phosphoprotein B-50, calmodulin-binding protein P-57, nerve growth-related peptide GAP43, neuromodulin, protein F1, pp46, B-50.
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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 MGSHMLCCMR RTKQVEKNDD DQKIEQDGIK PEDKAHKAAT KIQASFRGHI TRKKLKGEKK DDVQAAEAEA NKKDEAPVAD GVEKKGEGTT TAEAAPATGS KPDEPGKAGE TPSEEKKGEG DAATEQAAPQ APASSEEKAG SAETESATKA STDNSPSSKA EDAPAKEEPK QADVPAAVTA AAATTPAAED AAAKATAQPP TETGESSQAE ENIEAVDETK PKESARQDEG KEEEPEADQE HA
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 :
GOT2 Mouse, ActiveDescription:
Glutamic-Oxaloacetic Transaminase 2, Active Mouse Recombinant
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV, Kynurenine Aminotransferase 4.
Product # :
ENZ-1111Price :
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Description
GOT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (30-430 aa) and having a molecular mass of 46.8kDa.GOT2 is fused to a 21 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH7.4)
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 20 units/mg. Measured by the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C˚.
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Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 participates in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.
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Synonyms
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV, Kynurenine Aminotransferase 4.
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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 MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR
DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT
VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG
FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG
FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL
KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS
HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV TK
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.