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Search results

1000 results found for “Gliadin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    SPA-Cys

    Description:

    Staphylococcal Protein-A Cys Recombinant

    Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    Product # :

    PRO-1922

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    Description

    SPA-Cys Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 297 amino acids and having a molecular mass of 33.5kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    SPA protein was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by: (a) Analysis by HPLC.(b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.

    • Synonyms

      Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDC

    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.

    Spa Cys
  • View Data Sheet

    Name :

    DBNDD2 Human

    Description:

    Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 2 Human Recombinant

    Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.

    Product # :

    PRO-1167

    Price :

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    Description

    DBNDD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (1-161 a.a) and having a molecular mass of 20.1kDa (Molecular weight on SDS-PAGE will appear higher).DBNDD2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DBNDD2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dysbindin domain-containing protein 2 (DBNDD2) is a member of the dysbindin family. DBNDD2 regulates the activity of casein kinase-1 and inhibits CSNK1D autophosphorylation (in vitro). DBNDD2 also interacts with CSNK1D and CSNK1E. DBNDD2 is detected in brain.

    • Synonyms

      Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMDPNPR AALERQQLRL RERQKFFEDI LQPETEFVFP LSHLHLESQR PPIGSISSME VNVDTLEQVE LIDLGDPDAA DVFLPCEDPP PTPQSSGMDN HLEELSLPVP TSDRTTSRTS SSSSSDSSTN LHSPNPSDDG ADTPLAQSDE EEERGDGGAE PGACS.

    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.

    Dbndd2 Human
  • View Data Sheet

    Name :

    AMIGO2 Human

    Description:

    Adhesion Molecule with Ig-Like Domain 2 Human Recombinant

    Adhesion Molecule with Ig-Like Domain 2, Differentially Expressed in Gastric, Adenocarcinomas, AMIGO-2, ALI1, DEGA, Differentially Expressed in Gastric, Adenocarcinoma, Amphoterin-Induced Gene and Open Reading Frame 2, Transmembrane Protein AMIGO2, Amphoterin Induced Gene, Alivin 1, Alivin-1.

    Product # :

    PRO-2254

    Price :

    Quantity :

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    Description

    AMIGO2 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 367 amino acids (40-398a.a.) and having a molecular mass of 41.9kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).AMIGO2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    AMIGO2 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

    • Introduction

      Adhesion Molecule with Ig-Like Domain 2, also known as AMIGO2 is a member of the leucine-rich repeat family. AMIGO2 arbitrates homophilic in addition to heterophilic cell-cell interaction with AMIGO1 or AMIGO3. Furthermore, AMIGO2 contributes to signal transduction via its intracellular domain and is also essential for tumorigenesis of a subset of gastric adenocarcinomas.

    • Synonyms

      Adhesion Molecule with Ig-Like Domain 2, Differentially Expressed in Gastric, Adenocarcinomas, AMIGO-2, ALI1, DEGA, Differentially Expressed in Gastric, Adenocarcinoma, Amphoterin-Induced Gene and Open Reading Frame 2, Transmembrane Protein AMIGO2, Amphoterin Induced Gene, Alivin 1, Alivin-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      VCPTACICAT DIVSCTNKNL SKVPGNLFRL IKRLDLSYNR IGLLDSEWIP VSFAKLNTLI
      LRHNNITSIS TGSFSTTPNL KCLDLSSNKL KTVKNAVFQE LKVLEVLLLY NNHISYLDPS AFGGLSQLQK LYLSGNFLTQ FPMDLYVGRF KLAELMFLDV SYNRIPSMPM HHINLVPGKQ LRGIYLHGNP FVCDCSLYSL LVFWYRRHFS SVMDFKNDYT CRLWSDSRHS RQVLLLQDSF MNCSDSIING SFRALGFIHE AQVGERLMVH CDSKTGNANT DFIWVGPDNR LLEPDKEMEN FYVFHNGSLV IESPRFEDAG VYSCIAMNKQ RLLNETVDVT INVSNFTVSR SHAHEAFNTL EHHHHHH.

    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.

    Amigo2 Human
  • View Data Sheet

    Name :

    SERPINA5 Human

    Description:

    Serpin Peptidase Inhibitor Clade A Member 5 Human Recombinant

    PAI3, PCI, PROCI, PLANH3, Protein-C Inhibitor, Serpin A5, Plasminogen activator inhibitor 3, PAI-3, SERPINA5.

    Product # :

    PRO-749

    Price :

    Quantity :

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    • description
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    Description

    SERPINA5 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 408 amino acids (20-406 a.a.) and having a molecular mass of 45.9 kDa.The SERPINA5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
      SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease.

    • Synonyms

      PAI3, PCI, PROCI, PLANH3, Protein-C Inhibitor, Serpin A5, Plasminogen activator inhibitor 3, PAI-3, SERPINA5.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.

    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.

    Serpina5 Human
  • View Data Sheet

    Name :

    EDAR Human, Sf9

    Description:

    Ectodysplasin A Receptor Human Recombinant, Sf9

    Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

    Product # :

    PRO-2510

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    Description

    EDAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (27-187a.a.) and having a molecular mass of 45.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EDAR is expressed with a 249 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EDAR protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      ADPEYSNCGE NEYYNQTTGL CQECPPCGPG EEPYLSCGYG TKDEDYGCVP CPAEKFSKGG YQICRRHKDC EGFFRATVLT PGDMENDAEC GPCLPGYYML ENRPRNIYGM VCYSCLLAPP NTKECVGATS GASANFPGTS GSSTLSPFQH AHKELSGQGH LATAAAAFES ACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Edar Protein
  • View Data Sheet

    Name :

    ST6GALNAC5 Human

    Description:

    ST6GALNAC5 Human Recombinant

    Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5, GD1 alpha synthase, GalNAc alpha-2,6-sialyltransferase V, ST6GalNAc V, ST6GalNAcV, Sialyltransferase 7E, SIAT7-E, SIAT7E

    Product # :

    ENZ-1153

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    Description

    ST6GALNAC5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 316 amino acids (30-336a.a.) and having a molecular mass of 36.4kDa.ST6GALNAC5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ST6GALNAC5 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 or ST6GALNAC5, is part of the glycosyltransferase 29 group of proteins. ST6GALNAC5 is a sialyltransferase that takes part in the synthesis of ganglioside GD1a. This protein is part of the protein glycosylation transduction, meaning, modification of proteins. ST6GALNAC5 is expressed strictly in the brain tissue, and is a crucial component in breast cancer cells metastasis to the brain tissue. It is thought to enable cancer cells to go through the blood-brain barrier.

    • Synonyms

      Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5, GD1 alpha synthase, GalNAc alpha-2,6-sialyltransferase V, ST6GalNAc V, ST6GalNAcV, Sialyltransferase 7E, SIAT7-E, SIAT7E

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADLGGQKERP PQQQQQQQQQ QQQASATGSS QPAAESSTQQ RPGVPAGPRP LDGYLGVADH KPLKMHCRDC ALVTSSGHLL HSRQGSQIDQ TECVIRMNDA PTRGYGRDVG NRTSLRVIAH SSIQRILRNR HDLLNVSQGT VFIFWGPSSY MRRDGKGQVY NNLHLLSQVL PRLKAFMITR HKMLQFDELF KQETGKDRKI SNTWLSTGWF TMTIALELCD RINVYGMVPP DFCRDPNHPS VPYHYYEPFG PDECTMYLSH ERGRKGSHHR FITEKRVFKN WARTFNIHFF QPDWKPESLA INHPENKPVF HHHHHH

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    St6Galnac5 Human
  • View Data Sheet

    Name :

    CALML5 Human

    Description:

    Calmodulin Like 5 Human Recombinant

    CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5. 

    Product # :

    PRO-2475

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    Description

    CALML5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-146) containing 155 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 17.0kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    CALML5 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calmodulin Like 5, also known as CALML5 is a part of the calmodulin family of calcium binding proteins. CALML5 undergoes a conformational change as a result of binding calcium. CALML5 is taking part in terminal differentiation of keratinocytes and encodes a calcium binding protein expressed in the epidermis.

    • Synonyms

      CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • 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. CALML5 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS AGELTPEEEA QYKKAFSAVD TDGNGTINAQ ELGAALKATG KNLSEAQLRK LISEVDSDGD GEISFQEFLT AAKKARAGLE DLQVAFRAFD QDGDGHITVD ELRRAMAGLG QPLPQEELDA MIREADVDQD GRVNYEEFAR MLAQE.

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    Calml5 Human
  • View Data Sheet

    Name :

    CD47 Human

    Description:

    CD47 Human Recombinant

    CD47 Molecule, Antigenic Surface Determinant Protein OA3, CD47 Antigen (Rh-Related Antigen, Integrin-Associated Signal Transducer), Antigen Identified By Monoclonal Antibody 1D8, Integrin Associated Protein, Integrin-Associated Protein, Rh-Related Antigen, CD47 Glycoprotein, MER6, IAP, Integrin-Associated Signal Transducer, Leukocyte Surface Antigen CD47, CD47 Antigen, Protein MER6, OA3, CD47.

    Product # :

    PRO-2237

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    Description

    CD47 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-141 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 129 amino acids and having a molecular mass of 14.7kDa.CD47 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD47 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      CD47, functions in cell adhesions by performing as an adhesion receptor for THBS1 on platelets, furthermore CD47 plays a role in the modulation of integrins. In addition, CD47 takes a vital part in memory formation as well as synaptic plasticity in the hippocampus. Receptor for SIRPA avoids maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 prevents premature elimination of red blood cells, and it is also implicated in membrane permeability changes induced following virus infection.

    • Synonyms

      CD47 Molecule, Antigenic Surface Determinant Protein OA3, CD47 Antigen (Rh-Related Antigen, Integrin-Associated Signal Transducer), Antigen Identified By Monoclonal Antibody 1D8, Integrin Associated Protein, Integrin-Associated Protein, Rh-Related Antigen, CD47 Glycoprotein, MER6, IAP, Integrin-Associated Signal Transducer, Leukocyte Surface Antigen CD47, CD47 Antigen, Protein MER6, OA3, CD47.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      QLLFNKTKSV EFTFCNDTVV IPCFVTNMEA QNTTEVYVKW KFKGRDIYTF DGALNKSTVP TDFSSAKIEV SQLLKGDASL KMDKSDAVSH TGNYTCEVTE LTREGETIIE LKYRVVSWFS PNEHHHHHH.

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    Cd47 Human
  • View Data Sheet

    Name :

    PPIL4 Human

    Description:

    Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.

    Product # :

    ENZ-026

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    Description

    PPIL4 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 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPIL solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.

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    Ppil4 Human
  • View Data Sheet

    Name :

    CD96 Human

    Description:

    CD96 Human Recombinant

    CD96 Molecule, T Cell-Activated Increased Late Expression Protein, Cell Surface Antigen CD96, CD96 Antigen, T Cell Activation, Increased Late Expression, T-Cell Surface Protein Tactile, TACTILE.

    Product # :

    PRO-2445

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    Description

    CD96 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 490 amino acids (22-503a.a.) and having a molecular mass of 54.6kDa.CD96 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD96 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      CD96 is a type I membrane protein which is a part of the immunoglobulin superfamily. CD96 functions as cell markers in immune-phynotyping and participates in antigen presentation. CD96 plays a role in the adhesive interactions of activated T and NK cells through the late phase of the immune response.

    • Synonyms

      CD96 Molecule, T Cell-Activated Increased Late Expression Protein, Cell Surface Antigen CD96, CD96 Antigen, T Cell Activation, Increased Late Expression, T-Cell Surface Protein Tactile, TACTILE.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      VWEKTVNTEE NVYATLGSDV NLTCQTQTVG FFVQMQWSKV TNKIDLIAVY HPQYGFYCAY GRPCESLVTF TETPENGSKW TLHLRNMSCS VSGRYECMLV LYPEGIQTKI YNLLIQTHVT ADEWNSNHTI EIEINQTLEI PCFQNSSSKI SSEFTYAWSV EDNGTQETLI SQNHLISNST LLKDRVKLGT DYRLHLSPVQ IFDDGRKFSC HIRVGPNKIL RSSTTVKVFA KPEIPVIVEN NSTDVLVERR FTCLLKNVFP KANITWFIDG SFLHDEKEGI YITNEERKGK DGFLELKSVL TRVHSNKPAQ SDNLTIWCMA LSPVPGNKVW NISSEKITFL LGSEISSTDP PLSVTESTLD TQPSPASSVS PARYPATSSV TLVDVSALRP NTTPQPSNSS MTTRGFNYPW TSSGTDTKKS VSRIPSETYS SSPSGAGSTL HDNVFTSTAR AFSEVPTTAN GSTKTNHVHI TGIVVNKPKD GMLEHHHHHH.

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    Cd96 Human
  • View Data Sheet

    Name :

    GNB1 Human

    Description:

    Guanine Nucleotide Binding Protein Beta Polypeptide 1 Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein) Beta Polypeptide 1, Transducin Beta Chain 1, GNB1.

    Product # :

    PRO-1955

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    Description

    GNB1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 363 amino acids (1-340) and having a molecular mass of 39.8 kDa.GNB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GNB1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Heterotrimeric guanine nucleotide-binding proteins (G proteins) which integrate signals between receptors and effector proteins, are comprised of an alpha, a beta and a gamma subunit. The alpha, beta and gamma subunits are encoded by families of related genes. GNB1 encodes a beta subunit. Beta subunits are vital regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. G proteins are involved as a modulator or transducer in numerous transmembrane signaling systems. The beta and gamma chains are necessary for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein) Beta Polypeptide 1, Transducin Beta Chain 1, GNB1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSELDQL RQEAEQLKNQ IRDARKACAD ATLSQITNNI DPVGRIQMRT RRTLRGHLAK IYAMHWGTDS RLLVSASQDG KLIIWDSYTT NKVHAIPLRS SWVMTCAYAP SGNYVACGGL DNICSIYNLK TREGNVRVSR ELAGHTGYLS CCRFLDDNQI VTSSGDTTCA LWDIETGQQT TTFTGHTGDV MSLSLAPDTR LFVSGACDAS AKLWDVREGM CRQTFTGHES DINAICFFPN GNAFATGSDD ATCRLFDLRA DQELMTYSHD NIICGITSVS FSKSGRLLLA GYDDFNCNVW DALKADRAGV LAGHDNRVSC LGVTDDGMAV ATGSWDSFLK IWN.

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    Gnb1 Human
  • View Data Sheet

    Name :

    GNMT Human, Active

    Description:

    Glycine N-Methyltransferase Human Recombinant , Active

    Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.

    Product # :

    ENZ-1059

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    Description

    GNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a) and having a molecular mass of 34.9kDa.GNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GNMT protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

    • Synonyms

      Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20
      Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.

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    Gnmt Human Active
  • View Data Sheet

    Name :

    GPT Human

    Description:

    Glutamic-Pyruvate Transaminase Human Recombinant

    Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    Product # :

    ENZ-192

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    Description

    GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

    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.

    Gpt Human
  • View Data Sheet

    Name :

    CUEDC2 Human

    Description:

    CUE Domain Containing 2 Human Recombinant

    CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    Product # :

    PRO-1680

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    Description

    CUEDC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287) and having a molecular mass of 34 kDa.CUEDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CUEDC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 2 also known as CUEDC2 is a part of the CUEDC2 family and contains 1 CUE domain. CUEDC2 down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway and controls PGR protein levels through a parallel mechanism.

    • Synonyms

      CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMELERIV SAALLAFVQT HLPEADLSGL DEVIFSYVLG VLEDLGPSGP SEENFDMEAF TEMMEAYVPG FAHIPRGTIG DMMQKLSGQL SDARNKENLQ PQSSGVQGQV PISPEPLQRP EMLKEETRSS AAAAADTQDE ATGAEEELLP GVDVLLEVFP TCSVEQAQWV LAKARGDLEE AVQMLVEGKE EGPAAWEGPN QDLPRRLRGP QKDELKSFIL QKYMMVDSAE DQKIHRPMAP KEAPKKLIRY IDNQVVSTKG ERFKDVRNPE AEEMKATYIN LKPARKYRFH.

    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.

    Cuedc2 Human
  • View Data Sheet

    Name :

    HIF1AN Human

    Description:

    Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant

    FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.

    Product # :

    PRO-662

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    Description

    HIF1AN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349) and having a molecular mass of 40.2kDa. The HIF1AN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Overexpression of the HIF1AN is linked with tumor aggressiveness in pancreatic endocrine tumors. HIF1AN hydroxylates Notch ICD at two residues that are crucial for the function of Notch ICD as a transactivator within cells and during neurogenesis and myogenesis. HIF1AN is commonly expressed in invasive breast carcinoma. The hypoxic response and survival recommends that tumour regulation of HIF1AN is an additional important mechanism for HIF pathway activation. HIF1AN is an asparaginyl hydroxylase enzyme that controls the transcriptional activity of hypoxia-inducible factor. FIH1 is a part of the Fe2+ and 2-oxoglutarate-dependent dioxygenase superfamily, FIH1 is protein that hydoxylates a specific asparagine residue (Asn-803) within the HIF1A C-terminal transactivation domain. In normoxia, the HIF1AN-mediated hydroxylation of the HIF1? transactivation domain which results in blockage of the HIF1A-p300/CBP interaction and represses transcriptional activity of HIF1A targeted genes.

    • Synonyms

      FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN.

    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.

    Hif1An Human
  • View Data Sheet

    Name :

    sCD40L Human, His

    Description:

    soluble CD40 Ligand/TRAP Human Recombinant, His Tag

    CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L, CD40LG.

    Product # :

    CYT-670

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    Description

    CD40LG 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 169 amino acids (113-261 a.a.) and having a molecular mass of 18.3kDa. The CD40LG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CD40LG solution (0.5mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD40L or CD154 is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines. CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes. It also costimulates proliferation of activated T-cells and this is accompanied by the production of IFN-gamma , TNF-alpha , and IL2.

    • Synonyms

      CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L, CD40LG.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQKGDQNPQI AAHVISEASS KTTSVLQWAE KGYYTMSNNL VTLENGKQLT VKRQGLYYIY AQVTFCSNRE ASSQAPFIAS LCLKSPGRFE RILLRAANTH SSAKPCGQQS IHLGGVFELQ PGASVFVNVT DPSQVSHGTG FTSFGLLKL.

    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.

    Cd40L Human His
  • View Data Sheet

    Name :

    DCTN2 (1-403) Human

    Description:

    Dynactin 2 (1-403 a.a.) Human Recombinant

    Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.

    Product # :

    PRO-2303

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    Description

    Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403 a.a) and having a molecular mass of 46.9kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.

    • Synonyms

      Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEL EELTSTSVEH IIVNPNAAYD KFKDKRVGTK GLDFSDRIGK TKRTGYESGE YEMLGEGLGV KETPQQKYQR LLHEVQELTT EVEKIKTTVK ESATEEKLTP VLLAKQLAAL KQQLVASHLE KLLGPDAAIN LTDPDGALAK RLLLQLEATK NSKGGSGGKT TGTPPDSSLV TYELHSRPEQ DKFSQAAKVA ELEKRLTELE TAVRCDQDAQ NPLSAGLQGA CLMETVELLQ AKVSALDLAV LDQVEARLQS VLGKVNEIAK HKASVEDADT QSKVHQLYET IQRWSPIAST LPELVQRLVT IKQLHEQAMQ FGQLLTHLDT TQQMIANSLK DNTTLLTQVQ TTMRENLATV EGNFASIDER MKKLGK

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    Dctn2 1 403 Human
  • View Data Sheet

    Name :

    SERPINI1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant

    Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    Product # :

    PRO-213

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    Description

    SERPINI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 394 amino acids and having a total molecular mass of 44.7kDa. SERPINI1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by
    (a) Analysis by HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of rat C6 cells which is less than 0.5µg/ml, corresponding to a specific activity of >2000IU/mg.

    More Info

    • Introduction

      SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

    • Synonyms

      Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINI1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINI1 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 SERPINI1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG
      STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN
      GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL
      VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM
      MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT
      LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF
      IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL
      YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.

    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.

    Serpini1 Human
  • View Data Sheet

    Name :

    SH2D1A Human

    Description:

    SH2 domain containing 1A Human Recombinant

    SH2 domain-containing protein 1A, Duncan disease SH2-protein, Signaling lymphocytic activation molecule-associated protein, SLAM-associated protein, T-cell signal transduction molecule SAP, SH2D1A, DSHP, SAP, LYP, XLP, EBVS, IMD5, XLPD, MTCP1, FLJ18687, FLJ92177, SAP/SH2D1A.

    Product # :

    PRO-006

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    Description

    SH2D1A 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 148 amino acids (1-128 a.a.) and having a molecular mass of 16.3kDa. The SH2D1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SH2D1A solution (1 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SH2D1A acts as an inhibitor of the signaling lymphocyte activation molecule (SLAM) self-association. The SH2D1A protein is expressed at a high level in the thymus and the lung, with a lower level of expression in the spleen and the liver. The SH2D1A protein contains an SH2 domain and a short tail. SH2D1A has a key role in the bidirectional stimulation of T and B cells. Defects in the SH2D1A gene cause the X-linked lymphoproliferative disease (XLPD), aka Duncan disease. The XLPD is distinguished by a rare congenital immunodeficiency following an EBV infection (Epstein-Barr virus).

    • Synonyms

      SH2 domain-containing protein 1A, Duncan disease SH2-protein, Signaling lymphocytic activation molecule-associated protein, SLAM-associated protein, T-cell signal transduction molecule SAP, SH2D1A, DSHP, SAP, LYP, XLP, EBVS, IMD5, XLPD, MTCP1, FLJ18687, FLJ92177, SAP/SH2D1A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDAVAVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYHGY IYTYRVSQTE TGSWSAETAP GVHKRYFRKI KNLISAFQKP DQGIVIPLQY PVEKKSSARS TQGTTGIRED PDVCLKAP.

    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.

    Sh2D1A Human
  • View Data Sheet

    Name :

    CXCL14 Human

    Description:

    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-001

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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

    • 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.

    • Synonyms

      C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • 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.

    • 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.

    • 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.

    Cxcl14 Human
  • View Data Sheet

    Name :

    FAAH2 Human

    Description:

    Fatty Acid Amide Hydrolase 2 Human Recombinant

    Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

    Product # :

    ENZ-777

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    Description

    FAAH2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 524 amino acids (32-532a.a) and having a molecular mass of 57.4kDa. FAAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FAAH2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.

    • Synonyms

      Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSGGPKFAS KTPRPVTEPL LLLSGMQLAK LIRQRKVKCI DVVQAYINRI KDVNPMINGI VKYRFEEAMK EAHAVDQKLA EKQEDEATLE NKWPFLGVPL TVKEAFQLQG MPNSSGLMNR RDAIAKTDAT VVALLKGAGA IPLGITNCSE LCMWYESSNK IYGRSNNPYD LQHIVGGSSG GEGCTLAAAC SVIGVGSDIG GSIRMPAFFN GIFGHKPSPG VVPNKGQFPL AVGAQELFLC TGPMCRYAED LAPMLKVMAG PGIKRLKLDT KVHLKDLKFY WMEHDGGSFL MSKVDQDLIM TQKKVVVHLE TILGASVQHV KLKKMKYSFQ LWIAMMSAKG HDGKEPVKFV DLLGDHGKHV SPLWELIKWC LGLSVYTIPS IGLALLEEKL RYSNEKYQKF KAVEESLRKE LVDMLGDDGV FLYPSHPTVA PKHHVPLTRP FNFAYTGVFS ALGLPVTQCP LGLNAKGLPL GIQVVAGPFN DHLTLAVAQY LEKTFGGWVC PGKF.

    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.

    Faah2 Human
  • View Data Sheet

    Name :

    FAIM Human

    Description:

    Fas Apoptotic Inhibitory Molecule Human Recombinant

    FAIM1, Fas Apoptotic Inhibitory Molecule, FAIM2, LFG, NMP35, Fas Apoptotic Inhibitory Molecule 1, FAIM.

    Product # :

    PRO-1742

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    • More Info

    Description

    FAIM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-213aa) and having a molecular mass of 26.4kDa.FAIM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FAIM protein solution (0.5 mg /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

    • Introduction

      Fas apoptotic inhibitory molecule, also known as FAIM function as an inducible effector molecule which mediates Fas resistance produced by surface Ig engagement in B cells. In addition FAIM protects against death receptor-triggered apoptosis and regulates B-cell signaling and differentiation. Among the diseases associated with FAIM are hemorrhagic thrombocythemia, and food allergy.

    • Synonyms

      FAIM1, Fas Apoptotic Inhibitory Molecule, FAIM2, LFG, NMP35, Fas Apoptotic Inhibitory Molecule 1, FAIM.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMLLPFIR TLPLLCYNHL LVSPDSATLS PPYSLEKMTD LVAVWDVALS DGVHKIEFEH GTTSGKRVVY VDGKEEIRKE WMFKLVGKET FYVGAAKTKA TINIDAISGF AYEYTLEING KSLKKYMEDR SKTTNTWVLH MDGENFRIVL EKDAMDVWCN GKKLETAGEF VDDGTETHFS IGNHDCYIKA VSSGKRKEGI IHTLIVDNRE IPEIAS.

    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.

    Faim Human
  • View Data Sheet

    Name :

    ING1 Human

    Description:

    Inhibitor of Growth Family, Member 1 Human Recombinant

    Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    Product # :

    PRO-2130

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    ING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.3kDa.ING1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.

    • Synonyms

      Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMLSPANG EQLHLVNYVE DYLDSIESLP FDLQRNVSLM REIDAKYQEI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR.

    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.

    Ing1 Human
  • View Data Sheet

    Name :

    CCL16 Human

    Description:

    LEC/NCC-4 Human Recombinant

    C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    Product # :

    CHM-237

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    CCL16 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids and having a molecular mass of 11.2 kDa. The CCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL16 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    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 total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Human CCL16, also called HCC-4, liver-expressed chemokine (LEC), and lymphocyte and monocyte chemoattractant (LMC), is a novel CC chemokine recognized by bioinformatics. NCC-4 cDNA encodes a 120 amino acids along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. HCC4 is vaguely related to other CC chemokines, showing less than 30% sequence identity. Among CC chemokines, CCL-16 has the largest similarity to HCC-1. 2 potential polyadenylation signals are present on the human HCC-4 gene, and as a result, 2 transcripts containing roughly 1,500 base pairs and 500 base pairs have been detected. HCC-4 is expressed weakly by some lymphocytes, including NK cells, T cells, and some T cell clones. The expression of HCC-4 in monocytes is greatly upregulated in the presence of IL-10.
      CCL16 shows chemotactic activity for lymphocytes and monocytes rather than to neutrophils. NCC-4 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16 demonstrates chemotactic activity for monocytes and thp-1 monocytes, rather than for resting lymphocytes and neutrophils. HCC-4 induces a calcium flux in thp-1 cells that desensitized prior to the expression of rantes.

    • Synonyms

      C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL16 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 CCL16in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

    • Background

      What is the molecular weight/Mw of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein has a total Mw of 11.2kDa.

      What is the source or expression system of CCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL16 HUMAN Protein?
      Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL16 HUMAN Protein?
      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

      What applications can CCL16 HUMAN Protein be used in?
      CCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL16 HUMAN Protein?
      The endotoxin level is minimal, CCL16 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.

    Ccl16 Human
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