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1000 results found for “listeriolysin”
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Name :
EFNA3 HumanDescription:
Ephrin A3 Human Recombinant
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
Product # :
PRO-1460Price :
Quantity :
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Shipped with Ice Packs
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Description
EFNA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (23-214 a.a) and having a molecular mass of 24kDa. EFNA3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNA3 protein solution (1mg/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
EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.
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Synonyms
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQGPGG ALGNRHAVYW NSSNQHLRRE GYTVQVNVND YLDIYCPHYN SSGVGPGAGP GPGGGAEQYV LYMVSRNGYR TCNASQGFKR WECNRPHAPH SPIKFSEKFQ RYSAFSLGYE FHAGHEYYYI STPTHNLHWK CLRMKVFVCC ASTSHSGEKP VPTLPQFTMG PNVKINVLED FEGENPQVPK LEKSISG
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 :
CD226 HumanDescription:
CD226 Human Recombinant
DNAM-1, PTA1, TLiSA1, CD226 antigen, DNAX accessory molecule 1, DNAM1, Recombinant Human CD226.
Product # :
PRO-1353Price :
Quantity :
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Shipped with Ice Packs
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Description
CD226 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (19-254a.a.) and having a molecular mass of 29.4kDa.CD226 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CD226 protein solution (1mg/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
CD226 belongs to the Ig-superfamily containing 2 Ig-like domains of the V-set. CD226 is a 65kDa glycoprotein expressed on the surface NK cells, platelets, monocytes and a subset of T cells. CD226 facilitates cellular adhesion of platelets and megakaryocytic cells to vascular endothelial cells. CD226 also plays a role in megakaryocytic cell maturation.
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Synonyms
DNAM-1, PTA1, TLiSA1, CD226 antigen, DNAX accessory molecule 1, DNAM1, Recombinant Human CD226.
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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 MGSEEVLWHT SVPFAENMSL ECVYPSMGIL TQVEWFKIGT QQDSIAIFSP THGMVIRKPY AERVYFLNST MASNNMTLFF RNASEDDVGY YSCSLYTYPQ GTWQKVIQVV QSDSFEAAVP SNSHIVSEPG KNVTLTCQPQ MTWPVQAVRW EKIQPRQIDL LTYCNLVHGR NFTSKFPRQI VSNCSHGRWS VIVIPDVTVS DSGLYRCYLQ ASAGENETFV MRLTVAEGKT DNQYTLFVA.
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 :
KIR2DL1 HumanDescription:
Killer Cell Immunoglobulin-Like Receptor, 2 Domains Long Cytoplasmic Tail 1 Human Recombinant
Killer cell immunoglobulin-like receptor 2DL1, MHC class I NK cell receptor, Natural killer-associated transcript 1, NKAT-1, p58 natural killer cell receptor clones CL-42/47.11, p58 NK receptor, p58.1 MHC class-I-specific NK receptor, CD158 antigen-like family member A, CD158a antigen, KIR2DL1, CD158A, NKAT1, NKAT, p58.1, KIR221, KIR-K64.
Product # :
PRO-428Price :
Quantity :
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Shipped with Ice Packs
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Description
KIR2DL1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-202 and having a molecular mass of 22.2 kDa.The KIR2DL1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 25mM Tris- HCl (pH-7.5).
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
Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DL1 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, p58.1, cl-42, NKAT1, or KIR-K6), which recognizes class I MHC molecules (HLA-Cw2, -Cw4, -Cw5, and Cw6). The extracellular domain of KIR2DL1 was over expressed as insoluble protein aggregates (inclusion bodies). -
Synonyms
Killer cell immunoglobulin-like receptor 2DL1, MHC class I NK cell receptor, Natural killer-associated transcript 1, NKAT-1, p58 natural killer cell receptor clones CL-42/47.11, p58 NK receptor, p58.1 MHC class-I-specific NK receptor, CD158 antigen-like family member A, CD158a antigen, KIR2DL1, CD158A, NKAT1, NKAT, p58.1, KIR221, KIR-K64.
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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
MEGVHRKPSL LAHPGRLVKS EETVILQCWS DVMFEHFLLH REGMFNDTLR LIGEHHDGVS KANFSISRMT QDLAGTYRCY GSVTHSPYQV SAPSDPLDIV IIGLYEKPSL SAQLGPTVLA GENVTLSCSS RSSYDMYHLS REGEAHERRL PAGPKVNGTF QADFPLGPAT HGGTYRCFGS FHDSPYEWSK SSDPLLVSVT GN.
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 :
CD74 HumanDescription:
CD74 Human Recombinant
DHLAG, HLADG, Ia-GAMMA, li, HLA-DR antigens-associated invariant chain, p33, Ia antigen-associated invariant chain, HLA class II histocompatibility antigen gamma chain, CD74, Gamma Chain Of Class II Antigens, MHC HLA-DR Gamma Chain.
Product # :
PRO-1467Price :
Quantity :
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Shipped with Ice Packs
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Description
CD74 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (73-232 a.a) and having a molecular mass of 20.6kDa.CD74 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CD74 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CD74 (HLA class II histocompatibility antigen gamma chain isoform b), is a transmembrane protein (on antigen presenting cells) which is the invariant chain that chaperones MHC class IIdimers from the endoplasmic reticulum to the cell surface. CD74 is expressed by cells of both T lymphocyte and Blymphocyte lineages. CD74 upregulated in several cancers and is also expressed by non immune cells during inflammation. Diseases related with CD74 include thymic epithelial neoplasm and gastroduodenitis. Among its related super-pathways are Immune System and Immune response Antigen presentation by MHC class II. In addition CD74 functions as cell surface receptor for the cytokine MIF.
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Synonyms
DHLAG, HLADG, Ia-GAMMA, li, HLA-DR antigens-associated invariant chain, p33, Ia antigen-associated invariant chain, HLA class II histocompatibility antigen gamma chain, CD74, Gamma Chain Of Class II Antigens, MHC HLA-DR Gamma Chain.
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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 MGSQQQGRLD KLTVTSQNLQ LENLRMKLPK PPKPVSKMRM ATPLLMQALP MGALPQGPMQ NATKYGNMTE DHVMHLLQNA DPLKVYPPLK GSFPENLRHL KNTMETIDWK VFESWMHHWL LFEMSRHSLE QKPTDAPPKE SLELEDPSSG LGVTKQDLGP VPM
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 :
LECT1 HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1846Price :
Quantity :
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Shipped with Ice Packs
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.
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 :
CXCL3 HumanDescription:
GRO-Gamma Human Recombinant (CXCL3)
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
Product # :
CHM-310Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO-Gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7902 Dalton. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 CXCL3 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-Ser-Val-Val-Thr.
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Background
What is the molecular weight/Mw of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein has a total Mw of 7.9kDa.
What is the source or expression system of CXCL3 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL3 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.
What applications can CXCL3 HUMAN Protein be used in?
CXCL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 HUMAN Protein?
The endotoxin level is minimal, CXCL3 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BLyS HumanDescription:
B-cell Activating Factor Human Recombinant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-307Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.More Info
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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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 BAFF 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
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 17.7kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.
What is the amino acid sequence of BLYS Protein?
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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 :
ICOSLG HumanDescription:
Inducible T-Cell Costimulator Ligand Human Recombinant
Inducible T-Cell Costimulator Ligand, B7-Related Protein 1, B7 Homolog 2, B7-Like Protein Gl50, B7 Homologue 2, B7RP-1, ICOSL, B7-H2, B7RP1, B7H2, Transmembrane Protein B7-H2 ICOS Ligand, Inducible T-Cell Co-Stimulator Ligand, CD275 Antigen, ICOS Ligand, KIAA0653, ICOS-L, CD275, LICOS, GL50, ICOS ligand, B7 homolog 2, B7-H2, B7-like protein Gl50, B7-related protein 1, B7RP-1.
Product # :
PRO-2431Price :
Quantity :
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Shipped with Ice Packs
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Description
ICOSLG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 480 amino acids (19-256a.a.) and having a molecular mass of 53.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ICOSLG is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ICOSLG protein solution (1mg/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
Inducible T-Cell Costimulator Ligand also known as ICOSLG, is part of the B7 family of co-stimulatory molecules related to B7-1 and B7-2. ICOSLG is a transmembrane glycoprotein with extracellular IgV and IgC domains, in addition it binds to ICOS on activated T cells. The dependent signaling of ICOSLG takes part in a proliferative response.
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Synonyms
Inducible T-Cell Costimulator Ligand, B7-Related Protein 1, B7 Homolog 2, B7-Like Protein Gl50, B7 Homologue 2, B7RP-1, ICOSL, B7-H2, B7RP1, B7H2, Transmembrane Protein B7-H2 ICOS Ligand, Inducible T-Cell Co-Stimulator Ligand, CD275 Antigen, ICOS Ligand, KIAA0653, ICOS-L, CD275, LICOS, GL50, ICOS ligand, B7 homolog 2, B7-H2, B7-like protein Gl50, B7-related protein 1, B7RP-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
ADPDTQEKEV RAMVGSDVEL SCACPEGSRF DLNDVYVYWQ TSESKTVVTY HIPQNSSLEN VDSRYRNRAL MSPAGMLRGD FSLRLFNVTP QDEQKFHCLV LSQSLGFQEV LSVEVTLHVA ANFSVPVVSA PHSPSQDELT FTCTSINGYP RPNVYWINKT DNSLLDQALQ NDTVFLNMRG LYDVVSVLRI ARTPSVNIGC CIENVLLQQN LTVGSQTGND IGERDKITEN PVSTGEKNAA TLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.
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 :
BETV4Description:
Polcalcin Bet v 4 Recombinant
Polcalcin Bet v 4, Calcium-binding pollen allergen Bet v 4, Bet v 4, BETV4.
Product # :
ALR-017Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant BETV4 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 10,473 Dalton. BETV4 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
BETV4 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
BETV4 is primarily expressed in mature birch (Betula verrucosa) pollen and Causes an allergic reaction in human. BETV4 is a calcium-binding protein of 2-EF-hand type, which is exists in pollen of various plant species. This cross-reactivity can serve as a marker allergen for plant polysensitization.
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Synonyms
Polcalcin Bet v 4, Calcium-binding pollen allergen Bet v 4, Bet v 4, BETV4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
AminopeptidaseDescription:
Aminopeptidase Aeromonas Recombinant
Bacterial leucyl aminopeptidase, EC 3.4.11.10.
Product # :
ENZ-275Price :
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Shipped with Ice Packs
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Description
The 29 kDa Aeromonas Aminopeptidase is produced by genetic engineering and can be used for physical & structural investigations, sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at –X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.
Source
Aeromonas Proteolytica.
Formulation
Buffered solution containing 10mM Tris-HCl, 100mM NaCl and 5µM ZnSO4, pH 8.0.
Purity
Greater than 95.0% as determined by SEC-HPLC.
Biological Activity
Recombinant Aeromonas Aminopeptidase was found to have an activity of 108 Units/mg protein.
More Info
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Synonyms
Bacterial leucyl aminopeptidase, EC 3.4.11.10.
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Physical Appearance
Sterile filtered liquid formulation.
-
Stability
Two years when stored at -20°C, 2 weeks at 4°C.
-
Unit Definition
One unit of aminopeptidase activity is defined as the amount of enzyme that releases 1 μmole p-nitroaniline at 25°C in 1 minute.
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 :
ALCAM (CD166) HumanDescription:
Activated Leukocyte Cell Adhesion Molecule (CD166) Human Recombinant
Activated Leukocyte Cell Adhesion Molecule, CD166 Antigen, MEMD, Activated Leucocyte Cell Adhesion Molecule, CD166, ALCAM.
Product # :
PRO-2388Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
ALCAM Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 742 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa (Molecular size on SDS-PAGE will appear at approximately 70-100 kDa).CD166 is expressed with a 239 amino acid hIgGHis tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD166 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
-
Introduction
CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.
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Synonyms
Activated Leukocyte Cell Adhesion Molecule, CD166 Antigen, MEMD, Activated Leucocyte Cell Adhesion Molecule, CD166, ALCAM.
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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
ADPWYTVNSA YGDTIIIPCR LDVPQNLMFG KWKYEKPDGS PVFIAFRSST KKSVQYDDVP EYKDRLNLSE NYTLSISNAR ISDEKRFVCM LVTEDNVFEA PTIVKVFKQP SKPEIVSKAL FLETEQLKKL GDCISEDSYP DGNITWYRNG KVLHPLEGAV VIIFKKEMDP VTQLYTMTST
LEYKTTKADI QMPFTCSVTY YGPSGQKTIH SEQAVFDIYY PTEQVTIQVL PPKNAIKEGD NITLKCLGNG NPPPEEFLFY LPGQPEGIRS SNTYTLTDVR RNATGDYKCS LIDKKSMIAS TAITVHYLDL SLNPSGEVTR QIGDALPVSC TISASRNATV VWMKDNIRLR SSPSFSSLHY
QDAGNYVCET ALQEVEGLKK RESLTLIVEG KPQIKMTKKT DPSGLSKTII CHVEGFPKPA IQWTITGSGS VINQTEESPY INGRYYSKII ISPEENVTLT CTAENQLERT VNSLNVSANE NREKVNDQAK LIVGIVVGLL LAALEPKSCD 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 :
KLRD1 HumanDescription:
Killer Cell Lectin Like Receptor D1 Human Recombinant
Killer Cell Lectin Like Receptor D1, Killer Cell Lectin-Like Receptor Subfamily D, Member 1, NK Cell Receptor, CD94 Antigen, CD94, KP43, Killer Cell Lectin-Like Receptor Subfamily D Member 1, Natural Killer Cells Antigen CD94, KLRD1.
Product # :
PRO-2483Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
KLRD1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (32-179 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 157 amino acids and having a molecular mass of 18.2kDa.KLRD1 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLRD1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
KLRD1, also known as Killer Cell Lectin Like Receptor D1, is expressed on the surface of natural killer cells in the innate immune system. KLRD1 functions as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRD1 can create disulfide-bonded heterodimer with NKG2 family members. CD94 & NKG2 complex interacts with (HLA)-E, Human Leukocyte Antigen on target cells on the surface of natural killer cells.
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Synonyms
Killer Cell Lectin Like Receptor D1, Killer Cell Lectin-Like Receptor Subfamily D, Member 1, NK Cell Receptor, CD94 Antigen, CD94, KP43, Killer Cell Lectin-Like Receptor Subfamily D Member 1, Natural Killer Cells Antigen CD94, KLRD1.
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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
ADPKNSFTKL SIEPAFTPGP NIELQKDSDC CSCQEKWVGY RCNCYFISSE QKTWNESRHL CASQKSSLLQ LQNTDELDFM SSSQQFYWIG LSYSEEHTAW LWENGSALSQ YLFPSFETFN TKNCIAYNPN GNALDESCED KNRYICKQQL IHHHHHH
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 :
EBI3 MouseDescription:
Epstein Barr Virus Induced 3 Mouse Recombinant
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
Product # :
CYT-621Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 was lyophilized from 10mM Sodium Citrate pH-3.
Purity
Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 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
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
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Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 22.9kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.
What is the amino acid sequence of EBI3 Protein?
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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 :
SPOP HumanDescription:
Speckle-Type POZ Protein Human Recombinant
Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.
Product # :
PRO-195Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPOP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.
-
Synonyms
Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.
-
Physical Appearance
SPOP is supplied as a sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.
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 :
IL 16 Human, (130 a.a.)Description:
Interleukin-16 Human Recombinant, (130 a.a.)
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Product # :
CYT-536Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 13.5 kDa. The IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-16 was lyophilized at 1 mg/ml in 10mM NaP, pH-7.5.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis SDS-PAGE.Biological Activity
The ED50 as determined by its ability to chemoattract human CD4+ T lymphocytes using a concentration range of 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.More Info
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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4. -
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL16 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 Interleukin-16 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Asp-Leu-Asn.
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 :
STX2 HumanDescription:
Syntaxin-2 Human Recombinant
Syntaxin 2, epimorphin, EPM, EPIM, STX2A, STX2B, STX2C.
Product # :
PRO-1146Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STX2 Human Recombinant produced in E. coli is a single polypeptide chain containing 289 amino acids (1-264) and having a molecular mass of 33.6 kDa.STX2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The STX2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Syntaxin-2 (STX2) is a member of the syntaxin/epimorphin family of proteins. Syntaxin family members are cellular receptors for transport vesicles which participate in exocytosis in neutrophils. STX2 regulates epithelial-mesenchymal interactions and epithelial cell morphogenesis and activation. STX2 is a t-SNARE which localizes to the apical plasma membrane and intracellular vesicular structures. In addition, STX2, along with SNAP-23, is essential for regulated surfactant secretion.
-
Synonyms
Syntaxin 2, epimorphin, EPM, EPIM, STX2A, STX2B, STX2C.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMMRDRL PDLTACRKND DGDTVVVVEK DHFMDDFFHQ VEEIRNSIDK ITQYVEEVKK NHSIILSAPN PEGKIKEELE DLNKEIKKTA NKIRAKLKAI EQSFDQDESG NRTSVDLRIR RTQHSVLSRK FVEAMAEYNE AQTLFRERSK GRIQRQLEIT GRTTTDDELE EMLESGKPSI FTSDIISDSQ ITRQALNEIE SRHKDIMKLE TSIRELHEMF MDMAMFVETQ GEMINNIERN VMNATDYVEH AKEETKKAIK YQSKARRKK
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 :
Borrelia Spielmanii OspCDescription:
Borrelia Spielmanii Outer Surface Protein C Recombinant
Product # :
BOR-009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Borrelia Spielmanii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Borrelia Spielmanii OspC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Spielmanii OspC is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).
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Applications
Western blot with patient sample.
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 :
LMO1 HumanDescription:
LIM Domain Only 1 Human Recombinant
Rhombotin-1, Cysteine-rich protein TTG-1, LIM domain only protein 1, T-cell translocation protein 1, RBTN1, RHOM1, TTG1, LMO-1, LMO1.
Product # :
PRO-1457Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LMO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (1-156 a.a) and having a molecular mass of 20.2kDa.LMO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LMO1protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
LIM domain only 1 (LMO1) is a protein-coding gene. LMO1 encodes a transcriptional regulator which contains two cysteine-rich LIM domains but lacks a DNA-binding domain. LIM domains might play a part in protein interactions; hence the protein may regulate transcription by competitively binding to specific DNA-binding transcription factors.
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Synonyms
Rhombotin-1, Cysteine-rich protein TTG-1, LIM domain only protein 1, T-cell translocation protein 1, RBTN1, RHOM1, TTG1, LMO-1, LMO1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMMVLDKE DGVPMLSVQP KGKQKGCAGC NRKIKDRYLL KALDKYWHED CLKCACCDCR LGEVGSTLYT KANLILCRRD YLRLFGTTGN CAACSKLIPA FEMVMRARDN VYHLDCFACQ LCNQRFCVGD KFFLKNNMIL CQMDYEEGQL NGTFESQVQ
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 :
PRLR Human, AntagonistDescription:
Prolactin Receptor Antagonist Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
Biological Activity
fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).
More Info
-
Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
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Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
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 :
Y.Enterocolitica (O:9) YopEDescription:
Yersinia Enterocolitica (O:9) YopE Recombinant
Outer membrane virulence protein YopE, yopE, yop25.
Product # :
PRO-2576Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Yersinia Enterocolitica (O:9) YopE in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Y.Enterocolitica (O:9) YopE is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica (O:9) YopE is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
A main factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type 3 secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E is a GTPase activation protein which controls pore formation by activating small Rho GTPase, causing inhibition of actin polymerization.
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Synonyms
Outer membrane virulence protein YopE, yopE, yop25.
-
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. Avoid multiple freeze-thaw cycles.
-
Immunological Activity
Binds IgG- and IgM-type human antibodies.
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 :
Resistin Human (64-110)Description:
Resistin (64-110) Human Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
Product # :
CYT-1232Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Resistin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.
Resistin Function
Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.
Regulation
Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.
Clinical Relevance
Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.
Resistin Mechanism
Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.
Research
Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.
Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.
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 :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BD 1 RatDescription:
Beta Defensin -1 Rat Recombinant
Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.
Product # :
CYT-062Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.More Info
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Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
Beta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis. -
Synonyms
Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BD-1 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
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.
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Background
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 4.1kDa.
What is the source or expression system of BD1 Protein?
Escherichia Coli.
What is the Purity of BD1 Protein?
BD1 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BD1 Protein?
Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.
What is the amino acid sequence of BD1 Protein?
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.
What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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 :
IL 17 MouseDescription:
Interleukin-17 Mouse Recombinant
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Product # :
CYT-378Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-17 Murine Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 268 (2x134 a.a.) amino acids and having a molecular mass of 30 kDa. The IL-17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant induction of IL-6 production in cultured mouse NIH 3T3 fibroblasts was found to be 0.4 ng/ml, corresponding to a specific activity of 2,500,000 units/mg.More Info
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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
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Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17 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 17 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
MAAIIPQSSA CPNTEAKDFL QNVKVNLKVF NSLGAKVSSR RPSDYLNRST SPWTLHRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPESCPF TFRVEKMLVG VGCTCVASIV RQAA.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.942 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a standard solution of IL-17 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.