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Search results

1000 results found for “serum amyloid a”

Name

Description

Product #

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  • View Data Sheet

    Name :

    ANXA8L1 Human

    Description:

    Annexin A8 Like-1 Human Recombinant

    Annexin A8-like protein 2, bA145E20.2, ANXA8, annexin A8L2.

    Product # :

    PRO-1138

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    Description

    ANXA8L1 Human Recombinant produced in E. coli is a single polypeptide chain containing 351 amino acids (1-327) and having a molecular mass of 39.4 kDa.ANXA8L1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ANXA8L1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Annexin A8-like 2 (ANXA8L2) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Annexin family members are regulators of such varied processes such as ion flux, endocytosis and exocytosis, and cellular adhesion. ANXA8L2 is a membrane binding protein with various properties, including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion. ANXA8L2 overexpressionis linked to acute myelocytic leukemia. ANXA8L2 may act as an anticoagulant which indirectly inhibits the thromboplastin-specific complex.

    • Synonyms

      Annexin A8-like protein 2, bA145E20.2, ANXA8, annexin A8L2.

    • 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 MGSHMAWWKA WIEQEGVTVK SSSHFNPDPD AETLYKAMKG IGTNEQAIID VLTKRSNTQR QQIAKSFKAQ FGKDLTETLK SELSGKFERL IVALMYPPYR YEAKELHDAM KGLGTKEGVI IEILASRTKN QLREIMKAYE EDYGSSLEED IQADTSGYLE RILVCLLQGS RDDVSSFVDP ALALQDAQDL YAAGENIRGT DEMKFITILC TRSATHLLRV FEEYEKIANK SIEDSIKSET HGSLEEAMLT VVKCTQNLHS YFAERLYYAM KGAGTRDGTL IRNIVSRSEI DLNLIKCHFK KMYGKTLSSM IMEDTSGDYK NALLSLVGSD P

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

    Anxa8L2 Human
  • View Data Sheet

    Name :

    BCL2A1 Human

    Description:

    BCL2-Related Protein A1 Human Recombinant

    BCL2-related protein A1, Hemopoietic-specific early response protein, hematopoietic BCL2-related protein A1, Bcl-2-like protein 5, Protein BFL-1, BCL2L5, Protein GRS, HBPA1, ACC-1, ACC-2.

    Product # :

    PRO-1102

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    Description

    BCL2A1 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-152) and having a molecular mass of 20.2kDa.BCL2A1 is fused to a 24 amino acid His-tag at N-terminus & purified by conventional chromatography.

    Source

    E.coli.

    Formulation

    The BCL2A1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BCL2A1 delays apoptosis induced by IL-3 deficiency. BCL2A1 takes part in the response of hemopoietic cells to external signals and in preserving endothelial survival during infection.

    • Synonyms

      BCL2-related protein A1, Hemopoietic-specific early response protein, hematopoietic BCL2-related protein A1, Bcl-2-like protein 5, Protein BFL-1, BCL2L5, Protein GRS, HBPA1, ACC-1, ACC-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 MGSHMTDCEF GYIYRLAQDY LQYVLQIPQP GSGPSKTSRV LQKVAFSVQK EVEKNLKSCL DNVNVVSVDT ARTLFNQVME KEFEDDIINW GRIVTIFAFE GILIKKLLRQ QIAPDVDTYK EISYFVAEFI MNNTGEWIRQ NGGWENGFVK KFEPKS.

    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.

    Bcl2A1 Human
  • View Data Sheet

    Name :

    RAET1E Human, Sf9

    Description:

    Retinoic Acid Early Transcript 1E Human Recombinant, Sf9

    Retinoic Acid Early Transcript 1E, Lymphocyte Effector Toxicity Activation Ligand, RAE-1-Like Transcript 4, NKG2DL4, N2DL-4, LETAL, ULBP4, RL-4, NKG2D Ligand 4, BA350J20.7, RAET1E2, N2DL4.

    Product # :

    PRO-2467

    Price :

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    • description
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    Description

    RAET1E Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 204 amino acids (31-225 a.a.) and having a molecular mass of 23.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).RAET1E is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RAET1E 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.

    Citations

    More Info

    • Introduction

      RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

    • Synonyms

      Retinoic Acid Early Transcript 1E, Lymphocyte Effector Toxicity Activation Ligand, RAE-1-Like Transcript 4, NKG2DL4, N2DL-4, LETAL, ULBP4, RL-4, NKG2D Ligand 4, BA350J20.7, RAET1E2, N2DL4.

    • 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

      ADPHSLCFNF TIKSLSRPGQ PWCEAQVFLN KNLFLQYNSD NNMVKPLGLL GKKVYATSTW GELTQTLGEV GRDLRMLLCD IKPQIKTSDP STLQVEMFCQ REAERCTGAS WQFATNGEKS LLFDAMNMTW TVINHEASKI KETWKKDRGL EKYFRKLSKG DCDHWLREFL GHWEAMPEPT VSPVNASDIH WSSSSLPDHH HHHH.

    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.

    Raet1E Protein
  • View Data Sheet

    Name :

    EPM2A Antibody

    Description:

    Laforin, Mouse Anti Human

    Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.

    Product # :

    ANT-427

    Price :

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

    More Info

    • Introduction

      EPM2A is a dual-specificity phosphatase which associates with polyribosomes. The EPM2A protein may be involved in the regulation of glycogen metabolism. Mutations in the EPM2A gene have been linked to myoclonic epilepsy of Lafora.

    • Synonyms

      Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.

    • Immunogen

      Anti-human EPM2A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EPM2A amino acids 243-331 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P3F3AT.

    • Applications

      EPM2A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      EPM2A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Epm2A Antibody
  • View Data Sheet

    Name :

    LTA Antibody

    Description:

    Lymphotoxin-alpha, Mouse Anti Human

    Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, TNFB, TNFSF1, LT.

    Product # :

    ANT-014

    Price :

    Quantity :

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    • formulation
    • More Info
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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

    More Info

    • Introduction

      Lymphotoxin-alpha (LT-alpha or LTA) belongs to the TNF ligand superfamily, which bind the same TNF receptor and mediate similar pleiotropic effect. LTA is a proinflammatory cytokine with important biological activity and immunomodulatory function and is known to influence a variety of cellular response. Furthermore, LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses, is involved in the formation of secondary lymphoid organs during development and has a role in apoptosis. LTA is highly inducible, secreted, and forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA, which is located within the MHC III region of chromosome 6, shows close relation to the HLA class I (HLA-B) and class II (HLA-DR) genes. Polymorphism in the LTA gene appears to contribute to infectious disease susceptibility and infection. Genetic variations in the LTA gene are linked to susceptibility to leprosy type 4 and psoriatic arthritis.

    • Synonyms

      Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, TNFB, TNFSF1, LT.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human LTA mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LTA amino acids 35-205 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and ? light chain.

    • Clone

      PAT15A3AT.

    • Applications

      LTA antibody has been tested by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:250 ~ 500.
      Recommended starting dilution is 1:250.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      LTA antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Lta Antibody
  • View Data Sheet

    Name :

    BCL7A Human

    Description:

    B-cell CLL/lymphoma 7A Human Recombinant

    B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.

    Product # :

    PRO-1318

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    Description

    BCL7A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear higher).BCL7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCL7A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      B-cell CLL/lymphoma 7A (BCL7A) is a member of the BCL7 family. BCL7A is directly involved, with Myc and IgH, in a three-way gene translocation in a Burkitt lymphoma cell line. Thru gene translocation, the N-terminal region of the BCL7A gene is disrupted, which is assumed to be connected to the pathogenesis of a subset of high-grade B cell non-Hodgkin lymphoma. The N-terminal portion involved in the translocation includes the region which shares a compelling sequence similarity with those of BCL7B and BCL7C. Chromosomal anomalies involving BCL7A may be a cause of B-cell non-Hodgkin lymphoma.

    • Synonyms

      B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.

    • 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 MGSMSGRSVR AETRSRAKDD IKRVMAAIEK VRKWEKKWVT VGDTSLRIYK WVPVTEPKVD DKNKNKKKGK DEKCGSEVTT PENSSSPGMM DMHDDNSNQS SIADASPIKQ ENSSNSSPAP EPNSAVPSDG TEAKVDEAQA DGKEHPGAED ASDEQNSQSS MEHSMNSSEK VDRQPSGDSG LAAETSAISQ DLEGVPPSKK MKLEASQQNS EEM.

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    Bcl7A Human
  • View Data Sheet

    Name :

    MEP1A Human

    Description:

    Meprin A Subunit Alpha Human Recombinant

    Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.

    Product # :

    PRO-2349

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    Description

    MEP1A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 589 amino acids (22-601 a.a.) and having a molecular mass of 67.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MEP1A is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MEP1A protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Meprin A subunit alpha (MEP1A) is a single-pass type I membrane protein which is a member of the peptidase M12A family. MEP1A is abundantly expressed in the kidney and intestinal epithelial cells, is secreted into the urinary tract and intestinal lumen, and found in leukocytes and cancer cells under certain conditions. MEP1A is capable of proteolytically degrading extracellular matrix proteins, proteolytically processing bioactive proteins, and has a role in inflammatory processes.

    • Synonyms

      Meprin A Subunit Alpha, PABA Peptide Hydrolase, N-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Alpha, Meprin A, Alpha (PABA Peptide Hydrolase), Endopeptidase-2, EC 3.4.24.18, PPH Alpha, BA268F1.1 (Meprin A Alpha (PABA Peptide Hydrolase)), EC 3.4.24, PPHA, MEP1A.

    • 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

      ADPVPIKYLP EENVHDADFG EQKDISEINL AAGLDLFQGD ILLQKSRNGL RDPNTRWTFP IPYILADNLG LNAKGAILYA FEMFRLKSCV DFKPYEGESS YIIFQQFDGC WSEVGDQHVG QNISIGQGCA YKAIIEHEIL HALGFYHEQS RTDRDDYVNI WWDQILSGYQ HNFDTYDDSL ITDLNTPYDY ESLMHYQPFS FNKNASVPTI TAKIPEFNSI IGQRLDFSAI DLERLNRMYN CTTTHTLLDH CTFEKANICG MIQGTRDDTD WAHQDSAQAG EVDHTLLGQC TGAGYFMQFS TSSGSAEEAA LLESRILYPK RKQQCLQFFY KMTGSPSDRL VVWVRRDDST GNVRKLVKVQ TFQGDDDHNW KIAHVVLKEE QKFRYLFQGT KGDPQNSTGG IYLDDITLTE TPCPTGVWTV RNFSQVLENT SKGDKLQSPR FYNSEGYGFG VTLYPNSRES SGYLRLAFHV CSGENDAILE WPVENRQVII TILDQEPDVR NRMSSSMVFT TSKSHTSPAI NDTVIWDRPS RVGTYHTDCN CFRSIDLGWS GFISHQMLKR RSFLKNDDLI IFVDFEDITH LSQHHHHHH.

    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.

    MEP1A Human
  • View Data Sheet

    Name :

    RTCA Human

    Description:

    RNA 3'-Terminal Phosphate Cyclase Human Recombinant

    RNA 3'-terminal phosphate cyclase, RPC, RTC1, RTCD1, RNA cyclase, RNA-3'-phosphate cyclase, RNA terminal phosphate cyclase domain-containing protein 1, RTC domain-containing protein 1, RTCA, RPC1.

    Product # :

    PRO-2003

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    Description

    RTCA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 389 amino acids (1-366a.a) and having a molecular mass of 41.7kDa. RTCA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RTCA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RNA 3'-Terminal Phosphate Cyclase (RTCA) encodes a part of the RNA 3'-phosphate cyclase family. RTCA takes part in RNA metabolism by catalyzing the ATP-dependent conversion of the 3'-phosphate of RNA substrates to a 2',3'-cyclic phosphodiester. RTCA is involved in some phases of cellular RNA processing.

    • Synonyms

      RNA 3'-terminal phosphate cyclase, RPC, RTC1, RTCD1, RNA cyclase, RNA-3'-phosphate cyclase, RNA terminal phosphate cyclase domain-containing protein 1, RTC domain-containing protein 1, RTCA, RPC1.

    • 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 MGSMAGPRVE VDGSIMEGGG QILRVSTALS CLLGLPLRVQ KIRAGRSTPG LRPQHLSGLE MIRDLCDGQL EGAEIGSTEI TFTPEKIKGG IHTADTKTAG SVCLLMQVSM PCVLFAASPS ELHLKGGTNA EMAPQIDYTV MVFKPIVEKF GFIFNCDIKT RGYYPKGGGE VIVRMSPVKQ LNPINLTERG CVTKIYGRAF VAGVLPFKVA KDMAAAAVRC IRKEIRDLYV NIQPVQEPKD QAFGNGNGII IIAETSTGCL FAGSSLGKRG VNADKVGIEA AEMLLANLRH GGTVDEYLQD QLIVFMALAN GVSRIKTGPV TLHTQTAIHF AEQIAKAKFI VKKSEDEEDA AKDTYIIECQ GIGMTNPNL.

    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.

    Rtca Human
  • View Data Sheet

    Name :

    ANXA2 Human

    Description:

    Annexin A2 Human

    ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.

    Product # :

    PRO-1573

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    Description

    The Human Annexin A2 produced from Human Adipose Tissue has a molecular mass of 38.472kDa (calculated without glycosylation) containing 338 amino acid residues.

    Source

    Human Adipose Tissue.

    Formulation

    ANXA2 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl and pH 6.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ANXA2 is part of the annexin family and is involved in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein functions as an autocrine factor which increases osteoclast formation and bone resorption. ANXA2 is associated with sickle cell osteonecrosis. Reduced ANXA2 expression is associated with osteosarcoma metastases. ANXA2 is part of the putative cell surface vitamin D binding protein binding site complex and functions to mediate the chemotactic cofactor effect. ANXA2 is involved in dysferlin deficiency and in muscular dystrophies. Human colon adenocarcinoma cell differentiation is related with an up-regulation of ANXA2.

    • Synonyms

      ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      STVHEILCKL SLEGDHSTPP SAYGSVKAYT NFDAERDALN IETAIKTKGV DEVTIVNILT NRSNAQRQDI AFAYQRRTKK ELASALKSAL SGHLETVILG LLKTPAQYDA SELKASMKGL GTDEDSLIEI ICSRTNQELQ EINRVYKEMY KTDLEKDIIS DTSGDFRKLM VALAKGRRAE DGSVIDYELI DQDARDLYDA GVKRKGTDVP KWISIMTERS VPHLQKVFDR YKSYSPYDML ESIRKEVKGD LENAFLNLVQ CIQNKPLYFA DRLYDSMKGK GTRDKVLIRI MVSRSEVDML KIRSEFKRKY GKSLYYYIQQ DTKGDYQKAL LYLCGGDD.

    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.

    Human Anxa2
  • View Data Sheet

    Name :

    ASPA Human

    Description:

    Aspartoacylase Human Recombinant

    Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP

    Product # :

    ENZ-1135

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    Description

    ASPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-313) and having a molecular mass of 35.7 kDa.ASPA is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ASPA solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aspartoacylas or ASPA, is a protein, found in several tissues such as skeletal muscle, cerebral white matter, kidney, liver & lungs. ASPA is a homodimer that catalyses the deacetylation of Nacetylaspartic acid. In order to create L-aspartate & acetate.

    • Synonyms

      Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP

    • 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

      MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK LTLNAKSIRC CLH

    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.

    Aspartoacylase Human
  • View Data Sheet

    Name :

    SNRPA1 Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide A1 Human Recombinant

    U2 small nuclear ribonucleoprotein A', U2 snRNP A', SNRPA1, Lea1.

    Product # :

    PRO-1015

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    Description

    SNRPA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (1-255 a.a.) and having a molecular mass of 30.5kDa. SNRPA1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNRPA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl,2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      U2 small nuclear ribonucleoprotein A (SNRPA1), a 255 amino acid protein, is a component of the U2 snRNP which forms a complex with U2 snRNP B (U2B). U2 snRNP A and U2 snRNP B form together a complex which binds to the U2 snRNA hairpin IV. The configuration of the U2 snRNP A/U2 snRNP B dimer and the delicate variations of a few key residues regulate the snRNP-RNA-binding specificity.

    • Synonyms

      U2 small nuclear ribonucleoprotein A', U2 snRNP A', SNRPA1, Lea1.

    • 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 MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS DNEIRKLDGF PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL VELGDLDPLA SLKSLTYLSI LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV KLKERQEAEK MFKGKRGAQL AKDIARRSKT FNPGAGLPTD KKKGGPSPGD VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPTD DGEEEMEEDT VTNGS.

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    Snrpa1 Human
  • View Data Sheet

    Name :

    IL1A Porcine

    Description:

    Interleukin-1 Alpha Porcine Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    Product # :

    CYT-396

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    Description

    Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

    Citations

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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-1 alpha 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 Ser-Ala-Thr-Tyr-Ser.

    • Background

      What is the molecular weight/Mw of IL1A PORCINE Protein?
      IL1A PORCINE Protein has a total Mw of 18kDa.

      What is the source or expression system of IL1A PORCINE Protein?
      Escherichia Coli.

      What is the Purity of IL1A PORCINE Protein?
      IL1A PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A PORCINE Protein?
      The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

      What is the amino acid sequence of IL1A PORCINE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.

      What applications can IL1A PORCINE Protein be used in?
      IL1A PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1A PORCINE Protein?
      The endotoxin level is minimal, IL1A PORCINE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 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-1 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.

    Il 1 Alpha Porcine
  • View Data Sheet

    Name :

    IFN a 2b Human, Yeast

    Description:

    Interferon-Alpha 2b Human Recombinant, Yeast

    Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.

    Product # :

    CYT-460

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    Description

    Interferon-alpha 2b Human Recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of approximately 19.3 kDa.The IFN-a 2b is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH-7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x108IU/mg.

    Citations

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized glycosilated IFN-a 2b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2b 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 glycosilated IFN alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

    • Background

      What is the molecular weight/Mw of IFN A 2B HUMAN, YEAST Protein?
      IFN A 2B HUMAN, YEAST Protein has a total Mw of 19.3kDa.

      What is the source or expression system of IFN A 2B HUMAN, YEAST Protein?
      Saccharomyces cerevisiae.

      What is the Purity of IFN A 2B HUMAN, YEAST Protein?
      IFN A 2B HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN A 2B HUMAN, YEAST Protein?
      The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x108IU/mg.

      What is the amino acid sequence of IFN A 2B HUMAN, YEAST Protein?
      CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

      What applications can IFN A 2B HUMAN, YEAST Protein be used in?
      IFN A 2B HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN A 2B HUMAN, YEAST Protein?
      The endotoxin level is minimal, IFN A 2B HUMAN, YEAST 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.

    Interferon Alpha 2B Human Yeast
  • View Data Sheet

    Name :

    Activin-A Antibody

    Description:

    Activin-A, Polyclonal Rabbit Anti-Human Antibody

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    ANT-029

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    Formulation

    Lyophilized from a sterile filtered (0.2µm) solution containing phosphate buffered saline.

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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.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store at -20ºC. For long term storage freezes in working aliquots at -20ºC. Repeated freezing and thawing is not recommended.

    • Solubility

      Add 0.1 ml of distilled water and let the lyophilized pellet dissolve completely.

    • Immunogen

      Recombinant human Activin-A produced in plants.

    • Applications

      Activin-A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. In order to detect Human Activin A by indirect ELISA a dilution of at least 1:1,000 of the Activin A antibody is required. Activin A antibody, in conjunction with compatible secondary reagents (anti rabbit AP conjugated), allows the detection of 0.2-1 ng /well of Human Activin A. In order to detect human Activin A by WB analysis this IgG can be used in a dilution of 1:1,000.

    • Neutralization

      To yield one-half maximal inhibition (ND50) of the biological activity of Activin A (7.5ng/ml), a concentration of 60-200ng/ml of the Activin-A antibody is required.

    • Type

      Polyclonal Rabbit Antibody.

    • Purification Method

      Purified IgG prepared by affinity chromatography on protein G.

    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.

    Activin A Antibody
  • View Data Sheet

    Name :

    OmpA

    Description:

    Outer Membrane Protein-A Bacterial Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-571

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    Description

    The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.

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    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.

    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.

    Outer Membrane Protein A
  • View Data Sheet

    Name :

    CEA Protein

    Description:

    Carcinoembryonic Antigen Human

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-2801

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    Description

    CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

    Source

    Liver tissue.

    Formulation

    CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    • 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.

    • Applications

      Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.

    • Background

      Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.

      Structural Complexity of CEA:

      CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.

      CEA in Cancer Biology:

      CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.

      Beyond Cancer: CEA in Development and Inflammation:

      While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.

      CEA as a Diagnostic and Therapeutic Target:

      The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

    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.

    Cea Human
  • View Data Sheet

    Name :

    HBsAg Native, ay

    Description:

    Hepatitis B Surface Antigen, Native ay

    Product # :

    HBS-003

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    Description

    HbsAg ay subtype purified Human Hepatitis B positive plasma, having a Mw weight corresponding to p24, gp27, p33 and gp36 as shown on SDS-PAGE.

    Source

    Human Hepatitis B positive plasma.

    Formulation

    Sterile Filtered solution containing 15mM NaN3, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV). The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins and is commonly referred to as the Australian Antigen. HBsAg is an essential parameter to diagnose hepatitis B disease in the clinic and to monitor antiviral treatment.

    • Physical Appearance

      Filtered opalscent solution.

    • Stability

      HBsAg should be stored at 4°C. DO NOT FREEZE.

    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.

    Hbsag Native Ay
  • View Data Sheet

    Name :

    IFN a 1b Human

    Description:

    Interferon-Alpha 1b Human Recombinant

    Product # :

    CYT-283

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    Description

    Interferon-alpha 1b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids and having a molecular mass of 19.5 kDa. The Interferon-alpha 1b gene was obtained from human leukocytes. The IFN-a 1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution (50ug/ml) in PBS, pH 7.4, containing 4% mannitol and 1% HSA.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 1 x 108 IU/ mg.

    Citations

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    • Introduction

      IFN-alpha 1b is produced by macrophages, IFN-alpha 1b has antiviral activities and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interferon alpha 1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 1b 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 IFN alpha 1b 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 Cys-Asp-Leu-Pro-Glu.

    • Background

      What is the molecular weight/Mw of IFNA1 B Protein?
      IFNA1 B Protein has a total Mw of 19.5kDa.

      What is the source or expression system of IFNA1 B Protein?
      Escherichia Coli.

      What is the Purity of IFNA1 B Protein?
      IFNA1 B Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA1 B Protein?
      The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 1 x 108 IU/ mg.


      What is the amino acid sequence of IFNA1 B Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Glu.
      What applications can IFNA1 B Protein be used in?
      IFNA1 B Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA1 B Protein?
      The endotoxin level is minimal, IFNA1 B 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.

    Interferon Alpha 1B Human
  • View Data Sheet

    Name :

    NOV Human (260-357)

    Description:

    Nephroblastoma Overexpressed (260-357 a.a.) Human Recombinant

    Igfbp9, igfbp-9.

    Product # :

    CYT-1234

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    Description

    The IGFBP9 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The IGFBP9 His-Tagged Fusion Protein, produced in E. coli, is a 18kDa protein containing 98 amino acid residues of the IGFBP9 Human, 260-357 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

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    • Synonyms

      Igfbp9, igfbp-9.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized IGFBP9 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Nephroblastoma Overexpressed (NOV) is a part of the CCN (CTGF/CYR61/NOV) family which takes an important part in tissue repair and cellular signaling, differentiation and growth. NOV takes part in angiogenesis, extracellular matrix remodeling and cellular adhesion. NOV is also involved in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and participates in both internal and external cell signaling. NOV is expressed in tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    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.

    Igfbp9 Human
  • View Data Sheet

    Name :

    HAV P2C-P3B

    Description:

    Hepatitis A Virus P2C-P3B Recombinant

    Product # :

    HAV-230

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    Description

    The E.Coli derived 53.7 kDa recombinant protein fused to a GST tag contains the P2C-P3B immunodominant regions, amino acids 1492-1606.

    Source

    Escherichia Coli.

    Formulation

    10mM Tris-HCl, pH 9.6, 0.1% SDS and 50% glycerol.

    Purity

    HAV P2C-P3B protein is >90% pure as determined by 10% PAGE (coomassie staining).

    Citations

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    • Introduction

      Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 aa, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 aa, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. Four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.

    • Stability

      HAV P2C-P3B Protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles

    • Applications

      HAV P2C-P3B antigen is suitable for ELISA and Western blots, excellent antigen for detection of HAV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera HAV-infected individuals.

    • Purification Method

      HAV P2C-P3B protein was purified by proprietary chromatographic technique.

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

    Hav P2C P3B
  • View Data Sheet

    Name :

    TNF a Mouse

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-252

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    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (c) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    Citations

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    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-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.

    • Solubility

      It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 calibrated solution of TNF-a 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.

    Tnf Alpha Mouse
  • View Data Sheet

    Name :

    PKAR-I alpha Human

    Description:

    Protein Kinase A regulatory subunit-1 alpha Human Recombinant

    cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, PRKAR1A PKR1, PRKAR1, CAR, CNC, CNC1, PKR1, ADOHR, PPNAD1, ACRDYS1.

    Product # :

    PKA-202

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    Description

    PKA regulatory subunit I a Human Recombinant is a dimeric 86kDa protein (the monomer is 381 aa 43kDa). PKAR-I alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PKA regulatory subunit-I alpha is supplied at a concentration of 0.8 mg/ml in 20mM MOPS (pH 7.0), 150mM NaCl, 1mM 2-mercaptoethanol and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      The Regulatory (R) subunit of Protein Kinase A (PKA) inhibits its kinase activity by shielding the Catalytic (C) subunit from physiological substrates. This inhibition is reversed in response to extra-cellular signals that increase cAMP levels in the cytoplasm. Upon cAMP binding to R, C is allosterically released from R, activating a spectrum of downstream signaling cascades. Crystallographic data indicated that a series of distinct conformational changes within CBD-A must occur to relay the cAMP signal from the cAMP binding site to the R:C interaction interface. One critical cAMP relay site within the CBD-A of R has been identified as Asp170 because the D170A mutation selectively reduces the negative cooperativity between the cAMP- and C-recognition sites (i.e. the KD for the R:C complex in the presence of cAMP is reduced by more than 12-fold), without significantly compromising the high affinity of R for both binding partners.

    • Synonyms

      cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, PRKAR1A PKR1, PRKAR1, CAR, CNC, CNC1, PKR1, ADOHR, PPNAD1, ACRDYS1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      PKAR-Ia should be stored at 4°C if entire vial will be used within 2-4 weeks. For long term storage it is recommended to store at -20°C. Avoid multiple freeze-thaw cycles.

    • Inhibitory Activity

      The cAMP-dependent protein kinase, regulatory subunit RIa reversibly inhibits the catalytic subunit Ca of the cAMP-dependent protein kinase PKA. The inhibition of the catalytic subunit can be reversed by the addition of the second messenger cAMP.

    • Antigen Amino Acid Sequence

      MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKEEAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPKDYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFSVSFIA GETVIQQGDE GDNFYVIDQGETDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTLRKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSAAVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLGPCSDILKRNI QQYNSFVSLS V

    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.

    Pkar I Alpha Human
  • View Data Sheet

    Name :

    TNF a Rat, His

    Description:

    Tumor Necrosis Factor-alpha Rat Recombinant, His Tag

    Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    Product # :

    CYT-900

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    • description
    • source
    • formulation
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    Description

    TNF a Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235a.a.) and having a molecular mass of 19.9kDa.TNF a is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF a protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    • 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 MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.

    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.

    Tnf A Rat His
  • View Data Sheet

    Name :

    IL3RA Mouse

    Description:

    Interleukin-3 Receptor Subunit Alpha Mouse Recombinant

    Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.

    Product # :

    CYT-1210

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    Description

    IL3RA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-331 a.a.) and fused to a 231 a.a. Human IgG His Tag at C-terminus containing a total of 554 amino acids and having a molecular mass of 61.5 kDa.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL3RA protein solution (0.25mg/ml) contains 20mM Tris-HCL, 30% glycerol & 0.1M NaCl (pH-8).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.

    • Synonyms

      Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.

    • 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

      SDLAAVREAP PTAVTTPIQN LHIDPAHYTL SWDPAPGADI TTGAFCRKGR DIFVWADPGL ARCSFQSLSL CHVTNFTVFL GKDRAVAGSI QFPPDDDGDH EAAAQDLRCW VHEGQLSCQW ERGPKATGDV HYRMFWRDVR LGPAHNRECP HYHSLDVNTA GPAPHGGHEG CTLDLDTVLG STPNSPDLVP QVTITVNGSG RAGPVPCMDN TVDLQRAEVL APPTLTVECN GSEAHARWVA RNRFHHGLLG YTLQVNQSSR SEPQEYNVSI PHFWVPNAGA ISFRVKSRSE VYPRKLSSWS EAWGLVCPPE VMPVK LEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH

    • Background

      What is the molecular weight/Mw of IL 3 RA MOUSE Protein?
      IL 3 RA MOUSE Protein has a total Mw of 61.5kDa.

      What is the source or expression system of IL 3 RA MOUSE Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL 3 RA MOUSE Protein?
      IL 3 RA MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 3 RA MOUSE Protein?
      The biological functionality of IL 3 RA MOUSE Protein will be determined in the future.

      What is the amino acid sequence of IL 3 RA MOUSE Protein?
      SDLAAVREAP PTAVTTPIQN LHIDPAHYTL SWDPAPGADI TTGAFCRKGR DIFVWADPGL ARCSFQSLSL CHVTNFTVFL GKDRAVAGSI QFPPDDDGDH EAAAQDLRCW VHEGQLSCQW ERGPKATGDV HYRMFWRDVR LGPAHNRECP HYHSLDVNTA GPAPHGGHEG CTLDLDTVLG STPNSPDLVP QVTITVNGSG RAGPVPCMDN TVDLQRAEVL APPTLTVECN GSEAHARWVA RNRFHHGLLG YTLQVNQSSR SEPQEYNVSI PHFWVPNAGA ISFRVKSRSE VYPRKLSSWS EAWGLVCPPE VMPVK LEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

      What applications can IL 3 RA MOUSE Protein be used in?
      IL 3 RA MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 3 RA MOUSE Protein?
      The endotoxin level is minimal, IL 3 RA MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 3 RA MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 3 RA MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Il3Ra Mouse
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