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1000 results found for “oncostatin-m”
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Name :
RAN HumanDescription:
RAN, Member RAS Oncogene Family Human Recombinant
ARA24, Gsp1, TC4, GTP-binding nuclear protein Ran, GTPase Ran, Ras-related nuclear protein, Ras-like protein TC4, Androgen receptor-associated protein 24, Ras-like, RANP1.
Product # :
PRO-841Price :
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Shipped with Ice Packs
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Description
RAN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.5 kDa. The RAN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RAN Human solution containing 20mM Tris-HCl pH-8,1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
RAN is a GTP-binding protein that participates in nucleocytoplasmic transport. RAN is necessary for the import of protein into the nucleus and also for RNA export. RAN takes part in chromatin condensation and control of cell cycle. The RAN complex with BIRC5 participates in mitotic spindle formation by being as a physical scaffold to assist the delivery of the RAN effector molecule TPX2 to microtubules. RUN increases AR-mediated transactivation.
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Synonyms
ARA24, Gsp1, TC4, GTP-binding nuclear protein Ran, GTPase Ran, Ras-related nuclear protein, Ras-like protein TC4, Androgen receptor-associated protein 24, Ras-like, RANP1.
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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 MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL.
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 :
MEP1B MouseDescription:
Meprin A Beta Mouse Recombinant
Meprin A subunit beta (EC:3.4.24.63), Endopeptidase-2, Meprin B, Mep1b, Mep-1b.
Product # :
PRO-2313Price :
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Description
MEP1B produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 642 amino acids (21-654aa) and having a molecular mass of 72.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MEP1Bis expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
MEP1B protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Meprin A subunit beta (MEP1B) belongs to the astacin family of zinc endopeptidases 1, 2. MEP1B is a disulfide-linked, tetrameric metalloendopeptidase in renal brush border membranes. MEP1B is highly regulated, secreted cell-surface metalloendopeptidase, which is amply expressed in the kidney and intestine.
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Synonyms
Meprin A subunit beta (EC:3.4.24.63), Endopeptidase-2, Meprin B, Mep1b, Mep-1b.
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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
LPAPEKFVKD IDGGIDQDIF DINQGLGLDL FEGDIKLEAN GKNSIIGDHK RWPHTIPYVL EDSLEMNAKG VILNAFERYR LKTCIDFKPW SGEANYISVF KGSGCWSSVG NIHAGKQELS IGTNCDRIAT VQHEFLHALG FWHEQSRADR DDYVIIVWDR IQPGKEHNFN IYNDSVSDSL NVPYDYTSVM HYSKTAFQNG TESTIVTRIS EFEDVIGQRM DFSDYDLLKL NQLYNCTSSL SFMDSCDFEL ENICGMIQSS GDSADWQRVS QVLSGPESDH SKMGQCKDSG FFMHFNTSIL NEGATAMLES RLLYPKRGFQ CLEFYLYNSG SGNDQLNIYT REYTTGQQGG VLTLQRQIKE VPIGSWQLHY VTLQVTKKFR VVFEGLRGPG TSSGGLSIDD INLSETRCPH HIWHIQNFTQ ILGGQDTSVY SPPFYSSKGY AFQIYMDLRS STNVGIYFHL ISGANDDQLQ WPCPWQQATM TLLDQNPDIR QRMFNQRSIT TDPTMTSDNG SYFWDRPSKV GVTDVFPNGT QFSRGIGYGT TVFITRERLK SREFIKGDDI YILLTVEDIS HLNSTSAVPD PVPTLAVHNA CSEVVCQNGG ICVVQDGRAE CKCPAGEDWW YMGKRCEKRG STRDVEHHHH 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 :
IL1A Mouse, Sf9Description:
Interleukin-1 alpha Mouse Recombinant, Sf9
Il1a, Il-1a, Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-1062Price :
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Description
IL1AMouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (115-270a.a.) and having a molecular mass of 19.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL1A is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL1A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined in a cell proliferation assay using D10.G4.1 mouse helper T cells is < 0.15 ng/ml.
More Info
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Introduction
The cytokine IL-1 alpha or hematopoietin 1 is a member to the interleukin 1 family, encoded by the IL1A gene in humans. Essentially Il-1 is in charge of inflammation and the rising of fever and sepsis. In order to disturb the mentioned processes and treatment for diseases, inhibitors for Interleukin 1 alpha are being developed. Neutrophils and macrophages are the main activators of IL-1 alpha, as well as endothelial and epithelial cells. By binding to the il1 receptor it is a major part in the immune response regulation. In the activation process of tumor necrosis factor-alpha the IL1A has a part as well, and has physiological, metabolic and hematopoietic activities.
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Synonyms
Il1a, Il-1a, Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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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
ADPSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQISH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KLK13 Human, sf9Description:
Kallikrein-13 Human Recombinant, sf9
Kallikrein-Related Peptidase 13, KLKL4, Kallikrein-Like Protein 4, Kallikrein 13, KLK-L4, Kallikrein-Like Gene 4, Kallikrein-13, EC 3.4.21.-, EC 3.4.21, Kallikrein-13.
Product # :
ENZ-911Price :
Quantity :
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Shipped with Ice Packs
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Description
KLK13 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (17-277a.a.) and having a molecular mass of 29.7kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). KLK13 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK13 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 8,000 pmol/min/ug. One unit will hydrolyze 1.0 pmole of BAEE to Na-Benzoyl-L-arginine per minute at pH8.0 at 25C.More Info
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Introduction
Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.
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Synonyms
Kallikrein-Related Peptidase 13, KLKL4, Kallikrein-Like Protein 4, Kallikrein 13, KLK-L4, Kallikrein-Like Gene 4, Kallikrein-13, EC 3.4.21.-, EC 3.4.21, Kallikrein-13.
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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
GGVSQESSKV LNTNGTSGFL PGGYTCFPHS QPWQAALLVQ GRLLCGGVLV HPKWVLTAAH CLKEGLKVYL GKHALGRVEA GEQVREVVHS IPHPEYRRSP THLNHDHDIM LLELQSPVQL TGYIQTLPLS HNNRLTPGTT CRVSGWGTTT SPQVNYPKTL QCANIQLRSD EECRQVYPGK ITDNMLCAGT KEGGKDSCEG DSGGPLVCNR TLYGIVSWGD FPCGQPDRPG VYTRVSRYVL WIRETIRKYE TQQQKWLKGP QHHHHHH.
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 :
Resistin Human, HisDescription:
Resistin Human Recombinant, His Tag
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-256Price :
Quantity :
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Shipped with Ice Packs
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Description
Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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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.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.
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Name :
CRYAB MouseDescription:
Crystallin Alpha B Mouse Recombinant
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-018Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Recombinant CRYAB Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20 kDa. Mouse CRYAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse CRYAB protein solution contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVA AAPKK.
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 :
CRYGD MouseDescription:
Crystallin, Gamma D Mouse Recombinant
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
Product # :
PRO-2484Price :
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Shipped with Ice Packs
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Description
CRYGD Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-174 a.a.) and having a molecular mass of 23.5kDa.CRYGD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRYGD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRYGD is a member of the beta/gamma-crystallin family. Crystallins are the principal structural components of the vertebrate eye lens. The mammalian lens crystallins are divided into alpha, beta, and gamma families. Gamma-crystallins are involved in cataract formation. Defects in the CRYGD gene are responsible for cataract autosomal dominant (ADC), cataract congenital non-nuclear polymorphic autosomal dominant (CCP), cataract congenital cerulean type 3 (CCA3) and cataract crystalline aculeiform (CACA).
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Synonyms
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
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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 MGSMGKITFY EDRGFQGRHY ECSTDHSNLQ PYFSRCNSVR VDSGCWMLYE QPNFTGCQYF LRRGDYPDYQ QWMGFSDSVR SCRLIPHAGS HRIRLYEREE YRGQMIEFTE DCPSLQDRFH FNEIYSLNVL EGCWVLYDMT NYRGRQYLLR PGEYRRYHDW
GAMNARVGSL RRVMDFY
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 :
ACOT8 HumanDescription:
Acyl-CoA Thioesterase 8 Human Recombinant
Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.
Product # :
ENZ-712Price :
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Shipped with Ice Packs
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Description
ACOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.3kDa. ACOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACOT8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Acyl-CoA Thioesterase 8 (ACOT8) is a group of enzymes which catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), granting the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ACOT8 mediate Nef-induced down-regulation of CD4. ACOT8 contends with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 prefers medium-length fatty acyl-CoAs.
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Synonyms
Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.
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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 MGSMSSPQAP EDGQGCGDRG DPPGDLRSVL VTTVLNLEPL DEDLFRGRHY WVPAKRLFGG QIVGQALVAA AKSVSEDVHV HSLHCYFVRA GDPKLPVLYQ VERTRTGSSF SVRSVKAVQH GKPIFICQAS FQQAQPSPMQ HQFSMPTVPP PEELLDCETL IDQYLRDPNL QKRYPLALNR IAAQEVPIEI KPVNPSPLSQ LQRMEPKQMF WVRARGYIGE GDMKMHCCVA AYISDYAFLG TALLPHQWQH KVHFMVSLDH SMWFHAPFRA DHWMLYECES PWAGGSRGLV HGRLWRQDGV LAVTCAQEGV IRVKPQVSES KL.
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 :
MIEN1 HumanDescription:
Migration And Invasion Enhancer 1 Human Recombinant
C17orf37, C35, ORB3, RDX12, XTP4, HBV X-transactivated gene 4 protein, HBV XAg-transactivated protein 4, Protein C35, Migration and invasion enhancer 1.
Product # :
PRO-1657Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MIEN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (1-112 a.a.) and having a molecular mass of 14.5kDa.MIEN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIEN1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Migration And Invasion Enhancer 1 (MIEN1) is a member of the SelWTH family. MIEN1 enhances cell migration by stimulating filopodia formation at the leading edge of migrating cells and takes parts in regulation of apoptosis, probably via control of CASP3. MIEN1 participates in a redox-related process as well.
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Synonyms
C17orf37, C35, ORB3, RDX12, XTP4, HBV X-transactivated gene 4 protein, HBV XAg-transactivated protein 4, Protein C35, Migration and invasion enhancer 1.
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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 MGSMSGEPGQ TSVAPPPEEV EPGSGVRIVV EYCEPCGFEA TYLELASAVK EQYPGIEIES RLGGTGAFEI EINGQLVFSK LENGGFPYEK DLIEAIRRAS NGETLEKITN SRPPC.
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 :
MIP 1a MouseDescription:
Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
Product # :
CHM-320Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 1mg/ml solution containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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 Macrophage Inflammatory Protein-1a 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
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
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Background
What is the molecular weight/Mw of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein has a total Mw of 7.82kDa.
What is the source or expression system of MIP 1A MOUSE Protein?
Escherichia Coli.
What is the Purity of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A MOUSE Protein?
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of MIP 1A MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.
What applications can MIP 1A MOUSE Protein be used in?
MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A MOUSE Protein?
The endotoxin level is minimal, MIP 1A MOUSE 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 :
CTSE HumanDescription:
Cathepsin-E Human Recombinant
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.
Product # :
ENZ-776Price :
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Shipped with Ice Packs
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Description
CTSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and having a molecular mass of 35.4kDa.CTSE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CTSE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.
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Synonyms
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, 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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ SLTVGITVWD WPQQSPKEGP CVCACLSDRP
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 :
MOB1B HumanDescription:
MOB Kinase Activator 1B Human Recombinant
MOB Kinase Activator 1B, Mps One Binder Kinase Activator-Like 1A, Mob1 Homolog 1A, MOBKL1A, Mob1A, MOB4A, MOB1, Mps One Binder Kinase Activator-Like 1A (Yeast), MOB1, Mps One Binder Kinase Activator-Like 1A, MOB1 Mps One Binder Homolog B (Yeast), MOB1 Mps One Binder Homolog B, Mob4A Protein, MATS2, Mob1B, MOB kinase activator 1B.
Product # :
PKA-054Price :
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Description
MOB1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (1-216 a.a) and having a molecular mass of 27kDa. MOB1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
MOB1B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MOB Kinase Activator 1B (MOB1B) is similar to the yeast Mob1 protein. Yeast Mob1 binds Mps1p, which is a protein kinase vital for spindle pole body duplication and mitotic checkpoint regulation.
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Synonyms
MOB Kinase Activator 1B, Mps One Binder Kinase Activator-Like 1A, Mob1 Homolog 1A, MOBKL1A, Mob1A, MOB4A, MOB1, Mps One Binder Kinase Activator-Like 1A (Yeast), MOB1, Mps One Binder Kinase Activator-Like 1A, MOB1 Mps One Binder Homolog B (Yeast), MOB1 Mps One Binder Homolog B, Mob4A Protein, MATS2, Mob1B, MOB kinase activator 1B.
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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 MGSMSFLFGS RSSKTFKPKK NIPEGSHQYE LLKHAEATLG SGNLRMAVML PEGEDLNEWV AVNTVDFFNQ INMLYGTITD FCTEESCPVM SAGPKYEYHW ADGTNIKKPI KCSAPKYIDY LMTWVQDQLD DETLFPSKIG VPFPKNFMSV AKTILKRLFR VYAHIYHQHF DPVIQLQEEA HLNTSFKHFI FFVQEFNLID RRELAPLQEL IEKLTSKDR.
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 :
DCUN1D2 HumanDescription:
DCN1 Defective in Cullin Neddylation 1 Domain Containing 2 Human Recombinant
DCN1-like protein 2, DCUN1 domain-containing protein 2, Defective in cullin neddylation protein 1-like protein 2, DCUN1D2, C13orf17, DCUN1L2.
Product # :
PRO-899Price :
Quantity :
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Description
DCUN1D2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 32.3kDa.DCUN1D2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCUN1D2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DCN1-like protein 2 (DCUN1D2) which contains one DCUN1 domain and 1 UBA-like domain, may have a role in the neddylation of cullins which regulate SCF-type ubiquitin ligase complexes. The gene encoding Dcun1D2 is located on human chromosome 13. Chromosome 13 contains major tumor suppressor genes, including BRCA2 and RB1, which are linked with breast cancer susceptibility and retinoblastoma, respectively.
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Synonyms
DCN1-like protein 2, DCUN1 domain-containing protein 2, Defective in cullin neddylation protein 1-like protein 2, DCUN1D2, C13orf17, DCUN1L2.
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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 MHKLKSSQKD KVRQFMACTQ AGERTAIYCL TQNEWRLDEA TDSFFQNPDS LHRESMRNAV DKKKLERLYG RYKDPQDENK IGVDGIQQFC DDLSLDPASI SVLVIAWKFR AATQCEFSRK EFLDGMTELG CDSMEKLKAL LPRLEQELKD TAKFKDFYQF
TFTFAKNPGQ KGLDLEMAVA YWKLVLSGRF KFLDLWNTFL MEHHKRSIPR DTWNLLLDFG NMIADDMSNY DEEGAWPVLI DDFVEYARPV VTGGKRSLF.
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 :
NABP1 HumanDescription:
Nucleic Acid Binding Protein 1 Human Recombinant
Nucleic Acid Binding Protein 1, OBFC2A, Sensor Of Single-Strand DNA Complex Subunit B2, Single-Stranded DNA-Binding Protein 2, SSB2, Oligonucleotide/Oligosaccharide-Binding Fold Containing 2A, Nucleic Acid-Binding Protein 1, Oligonucleotide/Oligosaccharide-Binding Fold-Containing Protein 2A, Sensor Of SsDNA Subunit B2, SOSS-B2, SOSS Complex Subunit B2, hSSB2.
Product # :
PRO-1718Price :
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Description
NABP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a) and having a molecular mass of 24.8kDa.NABP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NABP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.2M, NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Nucleic acid binding protein 1 is a part of the SOSS complex, amultiprotein complex which functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint.In the SOSS complex, NABP1 acts as a sensor of single-stranded DNA which binds to single-stranded DNA, inparticular to polypyrimidines. The SOSS complex links with DNA lesions and affects diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair andmaintenance of genomic stability. NABP1 is essential for efficient homologous recombination-dependent repairof double-strand breaks (DSBs) and ATM-dependent signaling pathways.
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Synonyms
Nucleic Acid Binding Protein 1, OBFC2A, Sensor Of Single-Strand DNA Complex Subunit B2, Single-Stranded DNA-Binding Protein 2, SSB2, Oligonucleotide/Oligosaccharide-Binding Fold Containing 2A, Nucleic Acid-Binding Protein 1, Oligonucleotide/Oligosaccharide-Binding Fold-Containing Protein 2A, Sensor Of SsDNA Subunit B2, SOSS-B2, SOSS Complex Subunit B2, hSSB2.
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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 MGSMNRVNDP LIFIRDIKPG LKNLNVVFIV LEIGRVTKTK DGHEVRSCKV ADKTGSITIS VWDEIGGLIQ PGDIIRLTRG YASMWKGCLT LYTGRGGELQ KIGEFCMVYS EVPNFSEPNP DYRGQQNKGA QSEQKNNSMN SNMGTGTFGP VGNGVHTGPE SREHQFSHAG RSNGRGLINP QLQGTASNQT VMTTISNGRD PRRAFKR.
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 :
NCALD HumanDescription:
Neurocalcin Delta Recombinant Human
Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.
Product # :
PRO-093Price :
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Description
NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.
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Synonyms
Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.
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 :
Noggin HumanDescription:
Noggin Human Recombinant
SYM1, SYNS1, NOG.
Product # :
CYT-475Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC. -
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
- This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
- Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
- Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
- The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
- This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.
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 :
EFNA5 HumanDescription:
Ephrin A5 Human Recombinant
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2327Price :
Quantity :
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Description
EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNA5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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.
- View Data Sheet
Name :
IFNG Mouse, HisDescription:
Interferon-gamma Mouse Recombinant, His Tag
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-1001Price :
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- SDS-PAGE
Description
Interferon-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (23-155a.a.) and having a molecular mass of 18.2kDa.IFNG is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNG protein solution (0.5mg/ml) containing 20mM MES buffer (pH5.0), 1mM DTT, 0.2M NaCl & 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. -
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE, HIS Protein?
IFNG MOUSE, HIS Protein has a total Mw of 18.2kDa.
What is the source or expression system of IFNG MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE, HIS Protein?
IFNG MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE, HIS Protein?
The biological functionality of IFNG MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of IFNG MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.
What applications can IFNG MOUSE, HIS Protein be used in?
IFNG MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE, HIS Protein?
The endotoxin level is minimal, IFNG MOUSE, HIS 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 :
NUCB2 MouseDescription:
Nucleobindin-2 Mouse Recombinant
Nefa, Calnuc, AI607786, Nucleobindin-2, DNA-binding protein NEFA, Nucb2.
Product # :
PRO-605Price :
Quantity :
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Shipped with Ice Packs
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Description
NUCB2 Mouse Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain (amino acids 25-420) containing 417 amino acids and having a molecular mass of 49kDa.NUCB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 0.1M NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Nucleobindin-2 (NUCB2) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 is localized in neuronal perikarya and dendrites of mouse brain.
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Synonyms
Nefa, Calnuc, AI607786, Nucleobindin-2, DNA-binding protein NEFA, Nucb2.
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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 MVPIDVDKTK VHNTEPVENA RIEPPDTGLY YDEYLKQVIE VLETDPHFRE KLQKADIEEI RSGRLSQELD LVSHKVRTRL DELKRQEVGR LRMLIKAKLD ALQDTGMNHH LLLKQFEHLN HQNPNTFESR DLDMLIKAAT ADLEQYDRTR HEEFKKYEMMKEHERREYLK TLSEEKRKEE ESKFEEMKRK HEDHPKVNHP GSKDQLKEVW EETDGLDPND FDPKTFFKLH DVNNDGFLDE QELEALFTRE LEKVYNPQNA EDDMIEMEEE RLRMREHVMS EIDNNKDRLV TLEEFLRATE KKEFLEPDSW ETLDQQQLFT EDELKEYESI IAIQENELKKRAEELQKQKE DLQRQHDHLE AQKQEYHQAV QHLEQKKLQQ GIAPSGPAGE LKFEPHT.
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 :
OLR1 HumanDescription:
Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1.
Product # :
PRO-923Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
OLR1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (58-273) and having a molecular mass of 24.7 kDa.The OLR1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OLR1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.
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Synonyms
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1.
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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
MQLSQVSDLL TQEQANLTHQ KKKLEGQISA RQQAEEASQE SENELKEMIE TLARKLNEKS KEQMELHHQN LNLQETLKRV ANCSAPCPQD WIWHGENCYL FSSGSFNWEK SQEKCLSLDA KLLKINSTAD LDFIQQAISY SSFPFWMGLS RRNPSYPWLW EDGSPLMPHL FRVRGAVSQT YPSGTCAYIQ RGAVYAENCI LAAFSICQKK ANLRAQ
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 :
CCL24 RatDescription:
Eotaxin-2 Rat Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-282Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CCL24 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.2kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Rat Recombinant 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
VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.
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Background
What is the molecular weight/Mw of CCL24 RAT Protein?
CCL24 RAT Protein has a total Mw of 10.2kDa.
What is the source or expression system of CCL24 RAT Protein?
Escherichia Coli.
What is the Purity of CCL24 RAT Protein?
CCL24 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 RAT Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL24 RAT Protein?
VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.
What applications can CCL24 RAT Protein be used in?
CCL24 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 RAT Protein?
The endotoxin level is minimal, CCL24 RAT 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 :
CCL21 MouseDescription:
Exodus-2 Mouse Recombinant (CCL21)
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
Product # :
CHM-371Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Exodus-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids and having a molecular mass of 12kDa. The CCL21 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer and 0.15M NaCl pH-7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE & RP-HPLC.
Biological Activity
Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.
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Synonyms
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 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 Exodus2 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
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.
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Background
What is the molecular weight/Mw of CCL21 MOUSE Protein?
CCL21 MOUSE Protein has a total Mw of 12kDa.
What is the source or expression system of CCL21 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL21 MOUSE Protein?
CCL21 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL21 MOUSE Protein?
Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL21 MOUSE Protein?
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.
What applications can CCL21 MOUSE Protein be used in?
CCL21 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL21 MOUSE Protein?
The endotoxin level is minimal, CCL21 MOUSE 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 :
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 :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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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.
- View Data Sheet
Name :
PCMT1 HumanDescription:
Protein-L-Isoaspartate O-Methyltransferase Human Recombinant
EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.
Product # :
ENZ-522Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
PCMT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-227 a.a.) and having a molecular mass of 28.8 kDa. The PCMT1 is fused to a 36 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PCMT1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.
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Synonyms
EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.
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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
RGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAWK SGGASHSELI HNLRKNGIIK TDKVFEVMLA TDRSHYAKCN PYMDSPQSIG FQATISAPHM HAYALELLFD QLHEGAKALD VGSGSGILTA CFARMVGCTG KVIGIDHIKE LVDDSINNVR KDDPTLLSSG RVQLVVGDGR MGYAEEAPYD AIHVGAAAPV VPQALIDQLK PGGRLILPVG PAGGNQMLEQ YDKLQDGSIK MKPLMGVIYV PLTDKEKQWS RWK.
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.