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521 results found for “methylmalonic aciduria”
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Name :
DLL4 MouseDescription:
Delta-Like 4 Mouse Recombinant
Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.
Product # :
PRO-2236Price :
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Shipped with Ice Packs
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Description
DLL4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-532 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 512 amino acids and having a molecular mass of 55.8kDa.DLL4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DLL4 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Delta-Like4, also known as DLL4 is implicated in the Notch signaling pathway as Notch ligand. Consequently DLL4 negatively regulates endothelial cell proliferation, migration as well as angiogenic sprouting. DLL4 is vital for retinal progenitor proliferation and also required for suppressing rod fates in late retinal progenitors and for proper generation of other retinal cell types. Furthermore, at some stage in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.
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Synonyms
Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.
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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
GSGIFQLRLQ EFVNQRGMLA NGQSCEPGCR TFFRICLKHF QATFSEGPCT FGNVSTPVLG TNSFVVRDKN SGSGRNPLQL PFNFTWPGTF SLNIQAWHTP GDDLRPETSP GNSLISQIII QGSLAVGKIW RTDEQNDTLT RLSYSYRVIC SDNYYGESCS RLCKKRDDHF GHYECQPDGS LSCLPGWTGK YCDQPICLSG CHEQNGYCSK PDECICRPGW QGRLCNECIP HNGCRHGTCS IPWQCACDEG WGGLFCDQDL NYCTHHSPCK NGSTCSNSGP KGYTCTCLPG YTGEHCELGL SKCASNPCRN GGSCKDQENS YHCLCPPGYY GQHCEHSTLT CADSPCFNGG SCRERNQGSS YACECPPNFT GSNCEKKVDR CTSNPCANGG QCQNRGPSRT CRCRPGFTGT HCELHISDCA RSPCAHGGTC HDLENGPVCT CPAGFSGRRC EVRITHDACA SGPCFNGATC YTGLSPNNFV CNCPYGFVGS RCEFPVGLPP SFPWVAHHHH HH
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 :
ASRGL1 HumanDescription:
ASRGL1 Human Recombinant
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
Product # :
ENZ-837Price :
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Description
ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ASRGL1 protein solution (0.5mg/ml) containing Phosphate buffer saline, (pH 7.4) ,10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.
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Synonyms
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
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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 MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P.
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 :
ECHS1 Human, ActiveDescription:
Enoyl CoA Hydratase, Short chain, 1, Mitochondrial, Human Recombinant, Active
Enoyl-CoA Hydratase, Short Chain1, Enoyl Coenzyme A Hydratase, Short Chain, 1, Mitochondrial, Enoyl-CoA Hydratase, Short Chain, 1, Mitochondrial, Short Chain Enoyl-CoA Hydratase, EC 4.2.1.17, SCEH, Enoyl-CoA Hydratase, Mitochondrial, Short-Chain Enoyl-CoA Hydratase, Enoyl-CoA Hydratase 1, EC 4.2.1, ECHS1D, ECHS1 .
Product # :
ENZ-1046Price :
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Description
ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a) and having a molecular mass of 30.6kDa. ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ECHS1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% Glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 umole of crotonoyl-CoA to hydroxybutyryl-CoA per minute per minute at pH 7.5 at 25°C.
More Info
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Introduction
ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.
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Synonyms
Enoyl-CoA Hydratase, Short Chain1, Enoyl Coenzyme A Hydratase, Short Chain, 1, Mitochondrial, Enoyl-CoA Hydratase, Short Chain, 1, Mitochondrial, Short Chain Enoyl-CoA Hydratase, EC 4.2.1.17, SCEH, Enoyl-CoA Hydratase, Mitochondrial, Short-Chain Enoyl-CoA Hydratase, Enoyl-CoA Hydratase 1, EC 4.2.1, ECHS1D, ECHS1 .
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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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.
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 :
KCTD11 HumanDescription:
Potassium Channel Tetramerisation Domain Containing 11 Human Recombinant
C17orf36, KCASH1, MGC129844, REN, REN/KCTD11, KCTD11, BTB/POZ domain-containing protein KCTD11.
Product # :
PRO-1376Price :
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Description
KCTD11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-232a.a) and having a molecular mass of 28kDa. KCTD11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
KCTD11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Potassium Channel Tetramerisation Domain Containing 11 (KCTD11) is a 232 amino acid regulator of neuronal differentiation which induces growth arrest, apoptosis and the expression of p27 (cyclin-dependent kinase inhibitor). KCTD11 is expressed most highly in cerebellum. KCTD11 functions as an antagonist of the Hedgehog pathway and activator of the caspase cascade and among its related super-pathways are Melatonin Signaling and Activation of cAMP-Dependent PKA.
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Synonyms
C17orf36, KCASH1, MGC129844, REN, REN/KCTD11, KCTD11, BTB/POZ domain-containing protein KCTD11.
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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 MLGAMFRAGT PMPPNLNSQG GGHYFIDRDG KAFRHILNFL RLGRLDLPRG YGETALLRAE ADFYQIRPLL DALRELEASQ GTPAPTAALL HADVDVSPRL VHFSARRGPH HYELSSVQVD TFRANLFCTD SECLGALRAR FGVASGDRAE GSPHFHLEWA PRPVELPEVE YGRLGLQPLW TGGPGERREV VGTPSFLEEV LRVALEHGFR LDSVFPDPED LLNSRSLRFV RH.
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 :
CD276 HumanDescription:
CD276 Human Recombinant
CD276 Molecule, CD276 Antigen, Costimulatory Molecule, B7 Homolog 3, 4Ig-B7-H3, B7-H3, B7H3, B7RP-2.
Product # :
PRO-2456Price :
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Description
CD276 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (29-466a.a.) and having a molecular mass of 48.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CD276 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD276 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
CD276, belongs to the B7 family of immunoregulatory transmembrane glycoproteins expressed by T cells. CD276 is a costimulatory molecule for T cell activation in addition to IFN-gamma production. Furthermore CD276 upregulates BRCC3 expression, preventing DNA defects caused by 5-Fu. CD276 is correlated with TNM stage of NSCLC and act as a potential biomarker for NSCLC-derived MPEs. CD276 inhibits natural-killer mediated cell lysis in tumor cells, and act as a marker for detection of neuroblastoma cells. CD276 is implicated in the development of acute as well as chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. In addition, CD276 provides the placenta & fetus a proper immunological environment during the course of pregnancy.
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Synonyms
CD276 Molecule, CD276 Antigen, Costimulatory Molecule, B7 Homolog 3, 4Ig-B7-H3, B7-H3, B7H3, B7RP-2.
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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
LEVQVPEDPV VALVGTDATL CCSFSPEPGF SLAQLNLIWQ LTDTKQLVHS FAEGQDQGSA YANRTALFPD LLAQGNASLR LQRVRVADEG SFTCFVSIRD FGSAAVSLQV AAPYSKPSMT LEPNKDLRPG DTVTITCSSY QGYPEAEVFW QDGQGVPLTG NVTTSQMANE QGLFDVHSIL RVVLGANGTY SCLVRNPVLQ QDAHSSVTIT PQRSPTGAVE VQVPEDPVVA LVGTDATLRC SFSPEPGFSL AQLNLIWQLT DTKQLVHSFT EGRDQGSAYA NRTALFPDLL AQGNASLRLQ RVRVADEGSF TCFVSIRDFG SAAVSLQVAA PYSKPSMTLE PNKDLRPGDT VTITCSSYRG YPEAEVFWQD GQGVPLTGNV TTSQMANEQG LFDVHSVLRV VLGANGTYSC LVRNPVLQQD AHGSVTITGQ PMTFPPEALE 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 :
GLYAT HumanDescription:
Glycine-N-Acyltransferase Human Recombinant
Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.
Product # :
ENZ-148Price :
Quantity :
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Shipped with Ice Packs
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Description
GLYAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 36.0 kDa.The GLYAT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLYAT protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.
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Synonyms
Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.
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Physical Appearance
GLYAT is supplied as a 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 MMLPLQGAQM LQMLEKSLRK SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAA IKSFKVKQTQ RILYMAAETA KELTPFLLKS KILSPSGGKP KAINQEMFKL SSMDVTHAHL VNKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL.
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 :
CXCL8 Human (1-77)Description:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-327Price :
Quantity :
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Shipped at Room temp
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- sds-page
Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.sds-page
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 Interleukin 8 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
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.
What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.
What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
What applications can CXCL8 HUMAN (1-77) Protein be used in?
CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-77) 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 :
Midkine RatDescription:
Midkine Rat Recombinant
Midkine, MK, Mdk.
Product # :
CYT-747Price :
Quantity :
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Shipped at Room temp
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Description
Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.More Info
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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis. -
Synonyms
Midkine, MK, Mdk.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Midkine Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine Rat 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 Midkine Rat 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
VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.
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 :
CCL18 HumanDescription:
Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Product # :
CHM-322Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 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 MIP-4 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 of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
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Background
What is the molecular weight/Mw of CCL18 HUMAN Protein?
CCL18 HUMAN Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL18 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL18 HUMAN Protein?
CCL18 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL18 HUMAN Protein?
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL18 HUMAN Protein?
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
What applications can CCL18 HUMAN Protein be used in?
CCL18 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL18 HUMAN Protein?
The endotoxin level is minimal, CCL18 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.
- View Data Sheet
Name :
MX1 BovineDescription:
Myxovirus Resistance 1 Bovine Recombinant
Interferon-induced GTP-binding protein Mx1, Myxoma resistance protein 1, Myxovirus resistance protein 1, MX1, Interferon-Induced Protein P78, IFI-78K, IFI78, MxA.
Product # :
PRO-1662Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MX1 Bovine Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain (1-648 a.a) containing a total of 668 amino acids and having a molecular mass of 77kDa. The MX1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MX1 protein was lyophilized from a (1mg/ml) 0.2µm filtered solution containing 20mM Tris-HCl, pH7.9, 500mM NaCl, 0.5mM Imidazole, 0.1mM DTT and 6M urea.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Myxoma Resistance Protein 1 (MX1) is a member of the dynamin family and contains 1 GED domain. MX1 is an Interferon-induced dynamin-like GTPase with antiviral activity against rabies virus (RABV), vesicular stomatitis virus (VSV) and murine pneumonia virus (MPV). MX1 is ubiquitously expressed. MX1 is induced by type I and type III interferons.
-
Synonyms
Interferon-induced GTP-binding protein Mx1, Myxoma resistance protein 1, Myxovirus resistance protein 1, MX1, Interferon-Induced Protein P78, IFI-78K, IFI78, MxA.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MX1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MX1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized MX1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MGSSHHHHHHSSGLVPRGSHMVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCID
LIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLGNE
DEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHVPDLTLIDLP
GITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTI
GILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDH
AHFRDLLEEGKATIPCLAERLTSELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEES
EKMFCLIEKIDTFNKEIISTIEGEEFVEQYDSRLFTKVRAEFSKWSAVVEKNFEKGYEAIRKE
IKQFENRYRGRELPGFVNYKTFETIIKKQVRVLEEPAVDMLHTVTDIIRNTFTDVSGKHFNEF
FNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKNKKS
NHYFQSQVSEPSTDEIFQHLTAYQQEVSTRISGHIPLIIQFFVLRTYGEQLKKSMLQLLQDKD
QYDWLLKERTDTRDKRKFLKERLERLTRARQRLAKFPG.
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 :
IL36RN Human, HisDescription:
Interleukin-36 Receptor Antagonist Human Recombinant, His Tag
Interleukin 36 receptor antagonist, FIL1, FIL1(DELTA), FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, IL36RA, PSORP, FIL1 delta, Interleukin-1 HY1, IL-1 delta, Interleukin-1 receptor antagonist homolog 1, Interleukin-1-like protein 1, UNQ1896/PRO4342.
Product # :
CYT-844Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL36RN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (1-155 a.a) and having a molecular mass of 19.1kDa.IL36RN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL36RN protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.
-
Synonyms
Interleukin 36 receptor antagonist, FIL1, FIL1(DELTA), FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, IL36RA, PSORP, FIL1 delta, Interleukin-1 HY1, IL-1 delta, Interleukin-1 receptor antagonist homolog 1, Interleukin-1-like protein 1, UNQ1896/PRO4342.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVLSGALCFR MKDSALKVLY LHNNQLLAGG LHAGKVIKGE EISVVPNRWL DASLSPVILG VQGGSQCLSC GVGQEPTLTL EPVNIMELYL GAKESKSFTF YRRDMGLTSS FESAAYPGWF LCTVPEADQP VRLTQLPENG GWNAPITDFY FQQCD.
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 :
IRF1 HumanDescription:
IFN Regulatory Factor-1 Human Recombinant
IRF-1, IRF1, MAR.
Product # :
CYT-449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml in 20mM Tris pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
-
Synonyms
IRF-1, IRF1, MAR.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored 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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
-
Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.
What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 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.
- View Data Sheet
Name :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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 :
UBE2M HumanDescription:
Ubiquitin Conjugating Enzyme E2M Human Recombinant
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
Product # :
ENZ-345Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
UBE2M Human Recombinant produced E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.5kDa.UBE2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2M solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.
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Synonyms
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIKLFS LKQQKKEEES AGGTKGSSKK ASAAQLRIQK DINELNLPKT CDISFSDPDD LLNFKLVICP DEGFYKSGKF VFSFKVGQGY PHDPPKVKCE TMVYHPNIDL EGNVCLNILR EDWKPVLTIN SIIYGLQYLF LEPNPEDPLN KEAAEVLQNN RRLFEQNVQR SMRGGYIGST YFERCLK
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 :
M CSF HumanDescription:
Macrophage-Colony Stimulating Factor Human Recombinant
Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Product # :
CYT-308Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- biological activity
- More Info
Description
Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7x105 Units/mg.
More Info
-
Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.
-
Background
M-CSF (Macrophage-Colony Stimulating Factor) Human Recombinant: Unraveling Its Role in Macrophage Biology and Beyond
Abstract:
M-CSF (Macrophage-Colony Stimulating Factor), also known as Lanimostim, MCSF, or MGC31930, is a crucial growth factor that regulates the development, proliferation, and function of macrophages.
This research paper aims to provide a comprehensive analysis of the molecular characteristics, signaling pathways, and diverse physiological functions of M-CSF. Additionally, it explores the therapeutic implications of M-CSF in various diseases and disorders.
Synonyms such as Lanimostim, MCSF, and MGC31930 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a growth factor that plays a critical role in the regulation of macrophage biology. This section introduces M-CSF and its synonyms, highlighting their significance and relevance in scientific research.
Molecular Characteristics of M-CSF:
- This section explores the molecular characteristics of M-CSF, including its primary amino acid sequence, protein structure, and post-translational modifications. The importance of these factors in determining M-CSF's biological activity and receptor binding is discussed.
Signaling Pathways Activated by M-CSF:
- M-CSF activates specific signaling pathways upon binding to its receptor, leading to diverse cellular responses. This section focuses on the activation of the MAPK/ERK and PI3K/Akt pathways. The downstream effectors and transcriptional regulators involved in mediating M-CSF's cellular responses are also discussed.
Physiological Functions of M-CSF:
- M-CSF plays critical roles in various physiological processes, particularly in macrophage development, survival, polarization, and immune regulation. This section provides an in-depth analysis of M-CSF's contributions to these processes, emphasizing its role in hematopoiesis, tissue homeostasis, wound healing, and host defense.
Therapeutic Implications of M-CSF:
- The unique properties of M-CSF make it a promising therapeutic candidate for various diseases and disorders. This section discusses the potential applications of M-CSF in immunotherapy, tissue regeneration, cancer treatment, and autoimmune diseases. The challenges and future directions in utilizing M-CSF as a therapeutic agent are also explored.
M-CSF in Disease Pathogenesis:
- M-CSF dysregulation is implicated in the pathogenesis of several diseases, including cancer, inflammation, and bone disorders. This section examines the role of M-CSF in promoting tumor progression, macrophage-mediated inflammation, osteoclast differentiation, and metabolic diseases. The therapeutic implications and targeting of M-CSF in disease management are also discussed.
Conclusion:
- M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a critical growth factor involved in macrophage biology and disease pathogenesis. Understanding the molecular characteristics, signaling pathways, and physiological functions of M-CSF contributes to the exploration of its therapeutic potential in various disorders.
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 :
DCTN2 (1-403) HumanDescription:
Dynactin 2 (1-403 a.a.) Human Recombinant
Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.
Product # :
PRO-2303Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403 a.a) and having a molecular mass of 46.9kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEL EELTSTSVEH IIVNPNAAYD KFKDKRVGTK GLDFSDRIGK TKRTGYESGE YEMLGEGLGV KETPQQKYQR LLHEVQELTT EVEKIKTTVK ESATEEKLTP VLLAKQLAAL KQQLVASHLE KLLGPDAAIN LTDPDGALAK RLLLQLEATK NSKGGSGGKT TGTPPDSSLV TYELHSRPEQ DKFSQAAKVA ELEKRLTELE TAVRCDQDAQ NPLSAGLQGA CLMETVELLQ AKVSALDLAV LDQVEARLQS VLGKVNEIAK HKASVEDADT QSKVHQLYET IQRWSPIAST LPELVQRLVT IKQLHEQAMQ FGQLLTHLDT TQQMIANSLK DNTTLLTQVQ TTMRENLATV EGNFASIDER MKKLGK
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 :
FABP3 Human, HisDescription:
Fatty Acid Binding Protein 3 Human Recombinant, His Tag
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
Product # :
PRO-668Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FABP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 19.1 kDa. FABP3 is fused to a 37 amino acid His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP3 His-Tag is supplied in 20mM Tris-HCl pH 8.0 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.
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Synonyms
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
-
Physical Appearance
Sterile Filtered colorless liquid formulation.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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 :
ACE2 (19-740) HumanDescription:
Angiotensin Converting Enzyme 2 (19-740 a.a.), Human Recombinant
Product # :
ENZ-1122Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The CHO derived ACE2 Human recombinant protein contains the extracellular domain amino acids 19-740 fused to Fc tag at C-terminal. ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.
Source
CHO Cells
Formulation
ACE2 Human protein solution is supplied in 50mM Tris-HCl, pH7.5, and 90mM glycine.
Purity
Protein is >95% pure as determined SDS-PAGE.
Biological Activity
ACE2 activity was measured by its binding ability in a functional ELISA.
The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.
More Info
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Introduction
ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Purification Method
Purified by Protein-G chromatographic technique.
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 :
EPHB4 MouseDescription:
EPH Receptor B4 Mouse Recombinant
Ephrin type-B receptor 4 (EC:2.7.10.1), Developmental kinase 2, mDK-2, Hepatoma transmembrane kinase, Tyrosine kinase MYK-1, Ephb4, Htk, Mdk2, Myk1.
Product # :
PRO-2344Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EPHB4 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 532 amino acids (16-539 a.a.) and having a molecular mass of 58.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).EPHB4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPHB4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Ephrin type-B receptor 4 isoform b (Ephb4) belongs to the Eph receptor tyrosine kinase family which functions in neuronal guidance and mediate venal/arterial separation. EPHB4-mediated forward signaling regulates cellular repulsion and segregation form EFNB2-expressing cells. Furthermore, Ephb4 has a role in postnatal blood vessel remodeling, morphogenesis and permeability and is therefore essential in the context of tumor angiogenesis.
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Synonyms
Ephrin type-B receptor 4 (EC:2.7.10.1), Developmental kinase 2, mDK-2, Hepatoma transmembrane kinase, Tyrosine kinase MYK-1, Ephb4, Htk, Mdk2, Myk1.
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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
LEETLLNTKLETADLKWVTYPQAEGQWEELSGLDEEQHSVRTYEVCDMKRPGGQAHWLRT
GWVPRRGAVHVYATIRFTMMECLSLPRASRSCKETFTVFYYESEADTATAHTPAWMENPY
IKVDTVAAEHLTRKRPGAEATGKVNIKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYK
KCSWLITNLTYFPETVPRELVVPVAGSCVANAVPTANPSPSLYCREDGQWAEQQVTGCSC
APGYEAAESNKVCRACGQGTFKPQIGDESCLPCPANSHSNNIGSPVCLCRIGYYRARSDP
RSSPCTTPPSAPRSVVHHLNGSTLRLEWSAPLESGGREDLTYAVRCRECRPGGSCLPCGG
DMTFDPGPRDLVEPWVAIRGLRPDVTYTFEVAALNGVSTLATGPPPFEPVNVTTDREVPP
AVSDIRVTRSSPSSLILSWAIPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELR
GLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESESWREQLAVEHHHHHH.
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 :
LGALS13 HumanDescription:
Galectin-13 Human Recombinant
Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.
Product # :
CYT-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human LGALS13 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 16kDa. The LGALS13 also might appear as a homodimer, having a total Mw of 32kDa. LGALS13 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.
Source
Escherichia Coli.
Formulation
LGALS13 protein solution (0.5mg/ml) is formulated in 1xPBS buffer pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain (CRD) as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.
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Synonyms
Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.
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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
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN
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Background
What is the molecular weight/Mw of LGALS13 HUMAN Protein?
LGALS13 HUMAN Protein has a total Mw of 32kDa.
What is the source or expression system of LGALS13 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS13 HUMAN Protein?
LGALS13 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS13 HUMAN Protein?
The biological functionality of LGALS13 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS13 HUMAN Protein?
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN
What applications can LGALS13 HUMAN Protein be used in?
LGALS13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS13 HUMAN Protein?
The endotoxin level is minimal, LGALS13 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.
- View Data Sheet
Name :
SPARC Human, HisDescription:
Secreted Protein acidic & Rich in Cysteine Human Recombinant, His Tag
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Product # :
PRO-582Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Osteonectin Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 34 kDa.SPARC is expressed with a 6 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPARC (1 mg/ml) was lyophilized after extensive dialyses against 20mM 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
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
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Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Osteonectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BM-40 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 SPARC 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
MSYYHHHHHHPQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFD
DGAEETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCP
APIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCK
YIPPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTKQKLRVKKI
HENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGY
LSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQK
DIDKDLVI.
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
Description:
TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant, Active
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Product # :
CYT-1014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRAIL protein solution (1mg/ml) containing 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 1 ng/ml.
More Info
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Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. -
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
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Physical Appearance
Sterile Filtered colorless liquid.
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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
MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.
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 :
TPO Human, CHODescription:
Thrombopoietin Human Recombinant, CHO
MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.
Product # :
CYT-1070Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation. The TPO is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells.
Formulation
TPO protein solution contains phosphate buffered saline (pH7.4) and 2% albumin.
Purity
Greater than 98% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of MO7e cells corresponding to a specific activity of 3x105 units/mg.
More Info
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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.
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Synonyms
MPL Ligand, THCYT1, MPLLG, TPO, ML, Thrombopoietin Nirs Variant 1, MKCSF, Thrombopoietin, Myeloproliferative Leukemia Virus Oncogene Ligand, Megakaryocyte Growth and Development Factor, Megakaryocyte Colony-Stimulating Factor, C-Mpl Ligand, MGDF, Megakaryocyte Stimulating Factor, Prepro-Thrombopoietin.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Thrombopoietin although stable at room temperature for 1 week, should be stored between 2-8°C.
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 :
CTRB1 HumanDescription:
Chymotrypsinogen-B1, Human Recombinant
Product # :
ENZ-1016Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.
Source
E.coli
Formulation
The Human CTRB1 was lyophilized without any additives.
Purity
Greater than 95% as determined by HPLC.
Biological Activity
1100 units/mg protein.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.More Info
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Introduction
Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated 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 Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.
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.