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1000 results found for “calcium binding protein”

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  • View Data Sheet

    Description:

    Heat Shock 47kDa Human Recombinant

    HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.

    Product # :

    HSP-047

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    Description

    Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINH1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      SERPINH1 is part of the serpin superfamily of serine proteinase inhibitors. SEPINH1 expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen therefore it is a molecular chaperone which takes part in the maturation of collagen molecules, facilitating the folding and assembly of procollagen molecules, retaining unfolded molecules within the ER, and assisting the transport of correctly folded-molecules from the ER to Golgi apparatus. Autoantibodies to HSP47 protein have been found in rheumatoid arthritis. SERPINH1 binds specifically to collagen and acts as a chaperone in the biosynthetic pathway of collagen.

    • Synonyms

      HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAA EVKKPAAAAA PGTAEKLSPK AATLAERSAG LAFSLYQAMA KDQAVENILV SPVVVASSLG LVSLGGKATT ASQAKAVLSA EQLRDEEVHA GLGELLRSLS NSTARNVTWK LGSRLYGPSS VSFADDFVRS SKQHYNCEHS KINFRDKRSA LQSINEWAAQ TTDGKLPEVT KDVERTDGAL LVNAMFFKPH WDEKFHHKMV DNRGFMVTRS YTVGVMMMHR TGLYNYYDDE KEKLQIVEMP LAHKLSSLII LMPHHVEPLE RLEKLLTKEQ LKIWMGKMQK KAVAISLPKG VVEVTHDLQK HLAGLGLTEA IDKNKADLSR MSGKKDLYLA SVFHATAFEL DTDGNPFDQD IYGREELRSP KLFYADHPFI FLVRDTQSGS LLFIGRLVRP KGDKMRDEL.

    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.

    Serpinh1 Human
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    Description:

    Growth Hormone Binding Protein Rabbit Recombinant

    GHR, GHBP, GH receptor, Somatotropin receptor.

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    CYT-593

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    Description

    Growth Hormone Binding Protein Rabbit Extracellular Domain Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 249 amino acids and having a molecular mass of 28 kDa. GHBP Rabbit is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Growth Hormone Binding Protein Rabbit was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined bySDS-PAGE.

    Biological Activity

    Evidenced by its ability of forming 2:1 complex with non-primate Growth Hormones.

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    • Introduction

      GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

    • Synonyms

      GHR, GHBP, GH receptor, Somatotropin receptor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Binding Protein Rabbit although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP Rabbit 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 GHBP Rabbit in sterile 0.4% NaHCO3 pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AFSGSEATPATLGRASESVQRVHPGLGTNSSGKPKFTKCRSPELETFSCHWTDGVHHGLK
      SPGSVQLFYIRRNTQEWTQEWKECPDYVSAGENSCYFNSSYTSIWIPYCIKLTNNGGMVD
      QKCFSVEEIVQPDPPIGLNWTLLNVSLTGIHADIQVRWEPPPNADVQKGWIVLEYELQYK
      EVNETQWKMMDPVLSTSVPVYSLRLDKEYEVRVRSRQRSSEKYGEFSEVLYVTLPQMSPFTCEEDFRFP.

    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.

    Gh Receptor Rabbit
  • View Data Sheet

    Description:

    XIAP Associated Factor 1 Human Recombinant

    XIAP Associated Factor 1, BIRC4-Binding Protein, BIRC4BP, XIAPAF1, XIAP-Associated Factor 1, BIRC4 Binding Protein, HSXIAPAF1, XAF1.

    Product # :

    PRO-1963

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    Description

    XAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-125) and having a molecular mass of 18.6 kDa.XAF1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The XAF1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      XIAP Associated Factor 1 (XAF1) is a protein which binds to and counteracts the inhibitory effect of a member of the IAP (inhibitor of apoptosis) protein family. IAP proteins bind to and inhibit caspases which are activated in the course of apoptosis. The ratio of IAPs and proteins which interfere with their activity, such as the XAF1 protein, influence the progress of the apoptosis signaling pathway. Additionally, XAF1 inhibits anti-caspase activity of BIRC4. XAF1 induces cleavage and inactivation of BIRC4 independent of caspase activation. Furthermore, XAF1 mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells.

    • Synonyms

      XIAP Associated Factor 1, BIRC4-Binding Protein, BIRC4BP, XIAPAF1, XIAP-Associated Factor 1, BIRC4 Binding Protein, HSXIAPAF1, XAF1.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMEGD FSVCRNCKRH VVSANFTLHE AYCLRFLVLC PECEEPVPKE TMEEHCKLEH QQVGCTMCQQ SMQKSSLEFH KANECQERPV ECKFCKLDMQ LSKLELHESY CGSRTELCQG CGQFIMHRML A.

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    Xaf1 Human
  • View Data Sheet

    Description:

    Leucine Zipper And CTNNBIP1 Domain Containing Human Recombinant

    WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.

    Product # :

    PRO-1831

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    Description

    LZIC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (24-111) and having a molecular mass of 12.1 kDa. LZIC is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      LZIC is a member of the CTNNBIP1 family. LZIC protein is universally expressed, with largest levels in kidney and up-regulated in various cases of gastric cancers. LZIC has no interaction with CTNNB1.

    • Synonyms

      WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.

    • 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 MGSMASRGKT ETSKLKQNLE EQLDRLMQQL QDLEECREEL DTDEYEETKK ETLEQLSEFN DSLKKIMSGN MTLVDELSGM QLAIQAAISQ AFKTPEVIRL FAKKQPGQLR TRLAEMDRDL MVGKLERDLY TQQKVEILTA LRKLGEKLTA DDEAFLSANA GAILSQFEKV STDLGSGDKI LALASFEVEK TKK.

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    Lzic Human
  • View Data Sheet

    Description:

    Integrin Binding Sialoprotein Human Recombinant, HEK

    Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.

    Product # :

    PRO-2793

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    Description

    IBSP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain (17-317 a.a) containing a total of 307 amino acids and having a molecular mass of 34.3 kDa. IBSP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The IBSP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    >40%, measured by the ability of the immobilized protein to support the adhesion of MCF7 human breast cancer cells. When cells are added to Human IBSP coated plates 3 ug/ml.

    More Info

    • Synonyms

      Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.

    • 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

      FSMKNLHRRV KIEDSEENGV FKYRPRYYLY KHAYFYPHLK RFPVQGSSDS SEENGDDSSE EEEEEEETSN EGENNEESNE DEDSEAENTT LSATTLGYGE DATPGTGYTG LAAIQLPKKA GDITNKATKE KESDEEEEEE EEGNENEESE AEVDENEQGI NGTSTNSTEA ENGNGSSGGD NGEEGEEESV TGANAEDTTE TGRQGKGTSK TTTSPNGGFE PTTPPQVYRT TSPPFGKTTT
      VEYEGEYEYT GANEYDNGYE IYESENGEPR GDNYRAYEDE YSYFKGQGYD GYDGQNYYHH QHHHHHH.

    • Background

      1. Structural Diversity: Research on IBSP often delves into its structural characteristics. IBSP is known for its rich sialic acid content and multiple functional domains, including an RGD cell-binding domain and polyglutamic acid stretches. These structural features enable IBSP to interact with various cells, affecting adhesion and migration.

      2. Mineralization Regulator: A significant focus of research is IBSP's role in mineralization. It acts as a nucleator for calcium phosphate crystals, providing a scaffold for bone formation. Understanding how IBSP influences mineralization is crucial for insights into bone health and diseases like osteoporosis.

      3. Cell Signaling: Research papers explore IBSP's involvement in cell signaling pathways. IBSP has been linked to angiogenesis, inflammation, and cellular differentiation. Investigating these signaling pathways sheds light on its broader physiological roles.

      4. Biomedical Implications: Studies often discuss the biomedical implications of IBSP. Researchers investigate its potential roles in bone disorders such as osteoporosis and periodontal disease. Additionally, IBSP's involvement in tumor metastasis and dental tissue regeneration is a subject of interest.

      5. Recombinant IBSP: The use of recombinant IBSP in research is a significant topic. Researchers utilize recombinant IBSP to explore its functions, interactions, and potential therapeutic applications. This allows for controlled experiments and insights into IBSP's behavior.

      6. Diagnostics and Therapeutics: Research papers may discuss the diagnostic and therapeutic potential of IBSP. Understanding its roles in health and disease can lead to the development of diagnostic markers and therapeutic interventions, particularly in the context of bone and dental health.

      7. Clinical Relevance: Some research may focus on the clinical relevance of IBSP. This could include studies on patient populations with IBSP mutations or alterations, aiming to understand how variations in IBSP may contribute to specific medical conditions.

    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.

    Ibsp Protein
  • View Data Sheet

    Description:

    Bone Morphogenetic protein-13 Human Recombinant

    Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    Product # :

    CYT-938

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    Description

    BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

    More Info

    • Introduction

      Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.

    • Synonyms

      Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

    • Background

      Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.

      Production of BMP-13 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.

      Potential Therapeutic Applications:

      BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of GDF6 Protein?
      GDF6 Protein has a total Mw of 27.1kDa.

      What is the source or expression system of GDF6 Protein?
      Escherichia Coli.

      What is the Purity of GDF6 Protein?
      GDF6 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF6 Protein?
      The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

      What is the amino acid sequence of GDF6 Protein?
      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

      What applications can GDF6 Protein be used in?
      GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF6 Protein?
      The endotoxin level is minimal, GDF6 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.

    Bmp13 Human
  • View Data Sheet

    Description:

    Actinin Alpha

    Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

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    PRO-518

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    Description

    Ultra pure Alpha Actinin having a Molecular mass of 95,000 Dalton.

    Source

    Chicken Gizzard.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

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    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

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    Alpha Actinin
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    Description:

    Calponin 1, Basic, Smooth Muscle Human Recombinant

    Calponin 1 basic smooth muscle, Calponin H1 smooth muscle, SMCC, Basic calponin, Sm-Calp, calponin-1.

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    PRO-1129

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    Description

    CNN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 305 amino acids (1-297) and having a molecular mass of 34.2 kDa.CNN1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CNN1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin.

    • Synonyms

      Calponin 1 basic smooth muscle, Calponin H1 smooth muscle, SMCC, Basic calponin, Sm-Calp, calponin-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

      MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGNNF MDGLKDGIIL CEFINKLQPG SVKKINESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV QSTLLALASM AKTKGNKVNV GVKYAEKQER KFEPGKLREG RNIIGLQMGT NKFASQQGMT AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPAHNHHA HNYYNSALEH HHHHH

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    Cnn1 Human
  • View Data Sheet

    Description:

    S100 Calcium Binding Protein A4, Mouse Anti Human

    Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    Product # :

    ANT-607

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      S100A4 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 belongs to the family of calcium binding proteins such as calmodulin and troponin C. S100A is composed of an alpha and beta chain whereas S100B is composed of two beta chains. S100 protein is also expressed in the antigen presenting cells such as the Langerhans cells in skin and interdigitating reticulum cells in the paracortex of lymph nodes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A4 may function in motility, invasion, and tubulin polymerization. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human s100A4 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human s100A4 protein 1-101 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT1C3AT.

    • Applications

      s100A4 antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      s100A4 antibody was purified from mouse ascetic fluids by protein-A affinity chromatography.

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    S100A4 Antibody
  • View Data Sheet

    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.

    More Info

    • 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

    Description:

    Bone Morphogenetic Protein-2 Human Recombinant

    BMP-2, BMP2A.

    Product # :

    CYT-261

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    Description

    Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing 2x115 amino acids and having a molecular mass of 26kDa. The BMP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP2 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.

    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 its ability to induce alkaline phosphatase production by ATDC-5 cells is 0.5-1.0 µg/ml.

    More Info

    • Introduction

      BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

    • Synonyms

      BMP-2, BMP2A.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP2 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 Bone Morphogenetic Protein-2 in sterile 20mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISM LYLDENEKVV LKNYQDMVVE GCGCR.

    • Background

      What is the molecular weight/Mw of BMP2 Protein?
      BMP2 Protein has a total Mw of 26kDa.

      What is the source or expression system of BMP2 Protein?
      Escherichia Coli.

      What is the Purity of BMP2 Protein?
      BMP2 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP2 Protein?
      The ED50 as determined by its ability to induce alkaline phosphatase production by ATDC-5 cells is 0.5-1.0 µg/ml.

      What is the amino acid sequence of BMP2 Protein?
      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISM LYLDENEKVV LKNYQDMVVE GCGCR.

      What applications can BMP2 Protein be used in?
      BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP2 Protein?
      The endotoxin level is minimal, BMP2 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 1.4 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 BMP-2 as a Reference Standard.

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    Bmp 2 Human
  • View Data Sheet

    Description:

    Growth Hormone Binding Protein Human Recombinant, Sf9

    GHR, GHBP, GHIP.

    Product # :

    CYT-1152

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    Description

    GHBP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264aa) and having a molecular mass of 29.4kDa.GHBP is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone. The ED50 for this effect is equal or less than 10ng/ml.

    More Info

    • Introduction

      Growth Hormone Binding Protein or GHR, is a protein, part of the cytokine receptor superfamily. GHR binds to 2 receptors, therefore it enhances signal transduction via dimerization of receptors. In elevated levels, growth hormone operates as an antagonist due to high variance in the binding sites affinities. The antagonist operation can be embellished even more when the binding site is reduced its affinity.

    • Synonyms

      GHR, GHBP, GHIP.

    • 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

      FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT
      CEEDFYLEHH HHHH

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    Ghr Protein
  • 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

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    Spa Cys
  • View Data Sheet

    Description:

    Fatty Acid Binding Protein-3 Human, Native

    Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    Product # :

    PRO-2794

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    Description

    FABP3 Human produced in Human cardiac muscle tissue having a molecular mass of 15kDa and is purified by proprietary chromatographic technique.

    Source

    Human heart tissue.

    Formulation

    FABP3 was lyophilized from 10mM Tris-HCl, pH 8.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fatty Acid Binding Protein-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP3 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 FABP3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      FABP3 is abundantly expressed in cardiac and skeletal muscle tissues, where it serves as a crucial mediator in the cellular handling of fatty acids. By facilitating the uptake, transport, and utilization of fatty acids, FABP3 ensures a steady supply of energy, making it indispensable for the high-energy-demanding heart and skeletal muscles. Beyond its role in energy metabolism, FABP3 has been implicated in diverse cellular processes, including inflammation, oxidative stress response, and cellular differentiation.

      Molecular Insights:

      At the molecular level, FABP3 exhibits a remarkable affinity for long-chain fatty acids. Its unique binding properties enable it to shuttle fatty acids to specific cellular compartments, such as mitochondria, for β-oxidation. Additionally, FABP3 is intricately involved in the regulation of gene expression, modulating the activity of various transcription factors and signaling pathways. Understanding these molecular intricacies is key to deciphering FABP3's diverse functions.

      Physiological Significance:

      In cardiac muscle, FABP3 plays a crucial role in myocardial energy metabolism. During periods of increased energy demand, such as cardiac stress or exercise, FABP3 ensures a rapid supply of fatty acids for ATP production. Its absence or dysfunction has been associated with impaired cardiac function and increased susceptibility to ischemic injury. In skeletal muscles, FABP3 contributes to the utilization of fatty acids as an energy source during sustained physical activity.

      Implications in Disease:

      Research indicates that alterations in FABP3 expression and function are linked to several pathological conditions. In cardiovascular diseases, FABP3 has emerged as a potential biomarker for myocardial infarction, reflecting myocardial damage. Moreover, studies have highlighted its involvement in insulin resistance, diabetes, and metabolic syndrome, emphasizing its significance in metabolic disorders.

      Therapeutic Prospects:

      The unique properties of FABP3 have garnered attention in drug development. Researchers are exploring FABP3-targeted therapies for cardiovascular diseases and metabolic disorders. Modulating FABP3 activity presents a promising avenue for managing conditions characterized by dysregulated fatty acid metabolism and oxidative stress.

      Conclusion:

      FABP3, the unassuming intracellular fatty acid chaperone, plays a central role in human physiology and disease. Its intricate involvement in energy metabolism, cellular signaling, and disease pathogenesis underscores its significance as a research subject. As our understanding of FABP3 deepens, it opens doors to innovative diagnostic approaches and therapeutic interventions, potentially impacting millions of lives worldwide.

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    Fabp 3 Human
  • View Data Sheet

    Description:

    Cold Inducible RNA Binding Protein Human Recombinant

    Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP, CIRBP, A18HNRNP, CIRP.

    Product # :

    PRO-746

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    Description

    CIRBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular mass of 20.8kDa.CIRBP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CIRBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cold inducible RNA-binding protein (CIRBP) has a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP localizes to the nucleus and contains one RRM (RNA recognition motif) domain. Expressed ubiquitously, CIRBP is believed to play a crucial role in the suppression of cellular proliferation in response to UV irradiation or extreme cold.

    • Synonyms

      Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP, CIRBP, A18HNRNP, CIRP.

    • 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 MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRGR GRGFSRGGGD RGYGGNRFES RSGGYGGSRD YYSSRSQSGG YSDRSSGGSY
      RDSYDSYATH NE.

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    Cirbp Human
  • View Data Sheet

    Description:

    Collagen Type IV Alpha 3 Binding Protein Human Recombinant

    COL4A3BP, FLJ20597, Collagen type IV alpha-3-binding protein, GPBP, STARD11, CERT, HCERT, CERTL, Ceramide Transfer Protein, Goodpasture antigen-binding protein, StAR-related lipid transfer protein 11, START domain-containing protein 11.

    Product # :

    PRO-837

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    Description

    COL4A3BP Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 290 amino acids (347-598 a.a.) and having a molecular mass of 33.1 kDa. The COL4A3BP is fused to 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COL4A3BP Human solution containing 20mM Tris HCL pH-8, 0.1M NaCl, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COL4A3BP is a kinase that particularly phosphorylates the N-terminal region of the non-collagenous domain of the alpha 3 chain of type IV collagen, recognized as the Goodpasture antigen that is the outcome of an autoimmune reaction directed at COL4A3BP. One isoform of COL4A3BP participates in ceramide intracellular transport.

    • Synonyms

      COL4A3BP, FLJ20597, Collagen type IV alpha-3-binding protein, GPBP, STARD11, CERT, HCERT, CERTL, Ceramide Transfer Protein, Goodpasture antigen-binding protein, StAR-related lipid transfer protein 11, START domain-containing protein 11.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWAGSMLH WPTSLPSGDA FSSVGTHRFV QKVEEMVQNH MTYSLQDVGG DANWQLVVEE GEMKVYRREV EENGIVLDPL KATHAVKGVT GHEVCNYFWN VDVRNDWETT IENFHVVETL ADNAIIIYQT HKRVWPASQR DVLYLSVIRK IPALTENDPE TWIVCNFSVD HDSAPLNNRC VRAKINVAMI CQTLVSPPEG NQEISRDNIL CKITYVANVN PGGWAPASVL RAVAKREYPK FLKRFTSYVQ EKTAGKPILF.

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    Col4A3Bp Human
  • View Data Sheet

    Description:

    Sex Hormone-Binding Globulin Human Recombinant

    Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.

    Product # :

    PRO-1603

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    Description

    SHBG Human Recombinant produced in CHO cells is a single, glycosylated, polypeptide chain containing a total of 428 amino acids, having a molecular mass of 46.79kDa (calculated), the SHBG is fused to a 6 a.a C-terminal His tag and also includes a myc-epitope.The Human SHBG is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    SHBG filtered solution at a concentration of 55.6µg/ml in certified FBS (Fetal Bovine Serum 5%).

    More Info

    • Introduction

      Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.

    • Synonyms

      Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.

    • Physical Appearance

      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

      AAQPARRARR TKLLLLLLLL LRHTRQGWAL RPVLPTQSAH DPPAVHLSNG PGQEPIAVMT FDLTKITKTS SSFEVRTWDP EGVIFYGDTN PKDDWFMLGL RDGRPEIQLH NHWAQLTVGA GPRLDDGRWH QVEVKMEGDS VLLEVDGEEV LRLRQVSGPL TSKRHPIMRI ALGGLLFPAS NLRLPLVPAL DGCLRRDSWL DKQAEISASA PTSLRSCDVE SNPGIFLPPG TQAEFNLRDI PQPHAEPWAF SLDLGLKQAA GSGHLLALGT PENPSWLSLH LQDQKVVLSS GSGPGLDLPL VLGLPLQLKL SMSRVVLSQG SKMKALALPP LGLAPLLNLW AKPQGRLFLG ALPGEDSSTS FCLNGLWAQG QRLDVDQALN RSHEIWTHSC PQSPGNGTDA SHSRGGPEQKLISEEDLNSA VDHHHHHH.

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    Shbg Human
  • View Data Sheet

    Description:

    CAMP Responsive Element Binding Protein 3-Like 2 Human Recombinant

    CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 2.

    Product # :

    PRO-2153

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    Description

    CREB3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-378 a.a) and having a molecular mass of 44kDa. CREB3L2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CREB3L2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAMP Responsive Element Binding Protein 3-Like 2, also known as CREB3L2 belongs to the oasis bZIP transcription factor family. Members of this family are able to dimerize however from homodimers only. CREB3L2 is a transcriptional activator. Translocations between CREB3L2 on chromosome 7 and the gene fused in sarcoma on chromosome 16 can be found in some tumors. One disease which is associated with CREB3L2 is myxofibrosarcoma.

    • Synonyms

      CAMP Responsive Element Binding Protein 3-Like 2, BBF2H7, CAMP-Responsive Element-Binding Protein 3-Like Protein 2, BBF2 Human Homolog On Chromosome 7, Cyclic AMP-Responsive Element-Binding Protein 3-Like Protein 2, Basic Transcription Factor 2, B-ZIB Transcription Factor, FUS/BBF2H7 Protein, TCAG_1951439, Cyclic AMP-responsive element-binding protein 3-like protein 2, cAMP-responsive element-binding protein 3-like protein 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 MGSMEVLESG EQGVLQWDRK LSELSEPGDG EALMYHTHFS ELLDEFSQNV LGQLLNDPFL SEKSVSMEVE PSPTSPAPLI QAEHSYSLCE EPRAQSPFTH ITSDSFNDDE VESEKWYLST DFPSTSIKTE PITDEPPPGL VPSVTLTITA ISTPLEKEEP PLEMNTGVDS SCQTIIPKIK LEPHEVDQFL NFSPKEAPVD HLHLPPTPPS SHGSDSEGSL SPNPRLHPFS LPQTHSPSRA APRAPSALSS SPLLTAPHKL QGSGPLVLTE EEKRTLIAEG YPIPTKLPLS KSEEKALKKI RRKIKNKISA QESRRKKKEY MDSLEKKVES CSTENLELRK KVEVLENTNR TLLQQLQKLQ TLVMGKVSRT CKLAGTQTGT C.

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    Creb3L2 Human
  • View Data Sheet

    Description:

    Myelin Basic Protein Human Recombinant

    Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.

    Product # :

    PRO-1713

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    Description

    MBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197) and having a molecular mass of 23.9kDa.MBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.

    • Synonyms

      Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.

    • 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 MGSMGNHAGK RELNAEKAST NSETNRGESE KKRNLGELSR TTSEDNEVFG EADANQNNGT SSQDTAVTDS KRTADPKNAW QDAHPADPGS RPHLIRLFSR DAPGREDNTF KDRPSESDEL QTIQEDSAAT SESLDVMASQ KRPSQRHGSK YLATASTMDH ARHGFLPRHR DTGILDSIGR FFGGDRGAPK RGSGKVSSEE

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    Mbp Protein
  • View Data Sheet

    Description:

    TP53RK Binding Protein Human Recombinant

    TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.

    Product # :

    PRO-1185

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    Description

    TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.

    • Synonyms

      TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.

    • 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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL

    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.

    Tprkb Human
  • View Data Sheet

    Description:

    UL16 Binding Protein 2 Human Recombinant, Sf9

    ULBP2, ALCAN-alpha, N2DL2, NKG2DL2, RAET1H, UL16 Binding Protein 2, Retinoic Acid Early Transcript 1H, UL16-Binding Protein 2, ALCAN-Alpha, NKG2D Ligand 2, N2DL-2.

    Product # :

    PRO-2378

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    Description

    ULBP2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (26-216a.a) and having a molecular mass of 22.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ULBP2 is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ULBP2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ULBP2 is a member of the MHC class I family. ULBP2 is ligand for the NKG2D receptor, composed with at least ULBP1 and ULBP3. ULBPs promote multiple signaling pathways in primary NK cells, triggering the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D encourages calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 cooperates with soluble CMV glycoprotein UL16. This cooperation is blocked with the NKG2D receptor, providing a mechanism in which CMV infected cells can escape the immune system. Additionally, UL16 causes ULBP2 to be held in the ER and cis-Golgi apparatus so that it does not reach the cell surface.

    • Synonyms

      ULBP2, ALCAN-alpha, N2DL2, NKG2DL2, RAET1H, UL16 Binding Protein 2, Retinoic Acid Early Transcript 1H, UL16-Binding Protein 2, ALCAN-Alpha, NKG2D Ligand 2, N2DL-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

      ADPGRADPHS LCYDITVIPK FRPGPRWCAV QGQVDEKTFL HYDCGNKTVT PVSPLGKKLN VTTAWKAQNP VLREVVDILT EQLRDIQLEN YTPKEPLTLQ ARMSCEQKAE GHSSGSWQFS FDGQIFLLFD SEKRMWTTVH PGARKMKEKW ENDKVVAMSF HYFSMGDCIG WLEDFLMGMD STLEPSAGAP LAMSHHHHHH.

    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.

    Ulbp2 Human Sf9
  • View Data Sheet

    Description:

    Allograft Inflammatory Factor 1 Human Recombinant

    AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.

    Product # :

    CYT-697

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    • sds-page

    Description

    AIF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.9kDa. AIF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E. Coli.

    Formulation

    The AIF1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    2mM DTT, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS PAGE.

    sds-page

    More Info

    • Introduction

      Human AIF1 protein shares 98% homology/identity with that of rat. AIF1 is expressed in macrophages and neutrophils. The expression of AIF1 transcripts is upregulated by IFN-g in rat macrophages. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. In quiescent cultured human vascular smooth muscle cells synthesis of AIF1 is induced by IFN-g, IL1b, and conditioned medium of T-cells. Overexpression of AIF1 in human VSMCs results in enhanced growth of these cells. AIF1 is expressed during apoptosis rat mammary gland and ventral prostate tissues. Allograft Inflammatory Factor 1 is expressed by several tumor-associated activated macrophages and microglial cells in rat and human gliomas. There is an evident relationship of AIF1-expressing activated macrophages and microglial cells with tumor malignancy in humans.

    • Synonyms

      AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.

    • Stability

      Store AIF1 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 MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.

    • Background

      Allograft Inflammatory Factor 1 Human Recombinant: Uncovering its Role in Immune Responses and Therapeutic Prospects

      1. Abstract

      This paper explores the Allograft Inflammatory Factor 1 Human Recombinant (AIF-1), a cytoplasmic, IFN-gamma-inducible calcium-binding protein involved in inflammation and immunity. We review the structure, biological roles, and involvement of AIF-1 in disease pathology. The therapeutic potential of AIF-1 in immune-related disorders is also explored.

      2. Introduction

      AIF-1, also known as IBA1, plays an important role in immune responses. It is associated with various immune cells, particularly macrophages, and has been implicated in numerous inflammatory and immune-related diseases. Understanding the function of AIF-1 could aid the development of novel therapeutic strategies.

      3. Structure and Signaling of AIF-1

      AIF-1 is a small 17 kDa protein with an EF-hand calcium-binding motif. Although the precise mechanism by which AIF-1 exerts its functions is not entirely clear, it is known to regulate the activation, migration, and proliferation of macrophages, key cells involved in immune responses.

      4. Biological Functions of AIF-1

      AIF-1 has been shown to play key roles in macrophage activation and function, which are central to inflammation and immunity. It is also implicated in cell survival, proliferation, and differentiation.

      5. AIF-1 in Disease Pathology

      AIF-1 has been associated with a range of inflammatory and immune-related diseases, including rheumatoid arthritis, atherosclerosis, and multiple sclerosis. It is also implicated in several cancers, further underscoring its broad physiological and pathological relevance.

      6. Therapeutic Potential of AIF-1

      Given its pivotal role in immune responses, AIF-1 presents an intriguing target for therapeutic interventions in immune-related diseases. Modulating the activity of AIF-1 could potentially alleviate pathological inflammation and autoimmunity.

      7. Conclusion and Future Perspectives

      Our knowledge of AIF-1 and its functions has significantly improved in recent years, but much remains to be discovered. Further research into AIF-1's exact molecular mechanisms and roles in disease will undoubtedly contribute to the development of novel therapeutic strategies.

      What is the molecular weight/Mw of AIF1 Protein?
      AIF1 Protein has a total Mw of 18.9kDa.

      What is the source or expression system of AIF1 Protein?
      Escherichia Coli.

      What is the Purity of AIF1 Protein?
      AIF1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of AIF1 Protein?
      The biological functionality of AIF1 Protein will be determined in the future.

      What is the amino acid sequence of AIF1 Protein?
      MGSSHHHHHH SSGLVPRGSH MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.

      What applications can AIF1 Protein be used in?
      AIF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for AIF1 Protein?
      The endotoxin level is minimal, AIF1 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.

    Aif1 Human
  • View Data Sheet

    Description:

    Guanine Nucleotide Binding Protein-G Alpha Inhibiting Activity Polypeptide 2 Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein), Alpha Inhibiting Activity Polypeptide 2, GTP-Binding Regulatory Protein Gi Alpha-2 Chain, Guanine Nucleotide-Binding Protein G(I), Alpha-2 Subunit, Adenylate Cyclase-Inhibiting G Alpha Protein, GNAI2B, H_LUCA16.1, GIP.

    Product # :

    PRO-1310

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    Description

    GNAI2 Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 42.0 kDa.GNAI2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GNAI2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNAI2 is an alpha subunit of guanine nucleotide binding proteins (G proteins) and holds a guanine nucleotide binding site. GNAI2 takes part in the hormonal regulation of adenylate cyclase. GNAI2 has varies transcript variants encoding different isoforms yet only two full-length isoforms were identified up to date.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein), Alpha Inhibiting Activity Polypeptide 2, GTP-Binding Regulatory Protein Gi Alpha-2 Chain, Guanine Nucleotide-Binding Protein G(I), Alpha-2 Subunit, Adenylate Cyclase-Inhibiting G Alpha Protein, GNAI2B, H_LUCA16.1, GIP.

    • 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 MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF.

    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.

    Gnai2 Human
  • View Data Sheet

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant, His Tag

    Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

    Product # :

    CYT-629

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    Description

    BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

    • 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

      MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

    • Background

      Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK

      Abstract:

      Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).

      Introduction:

      Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.

      BMP-7 HR Signaling in HEK Cells:

      Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.

      Influential Role in Cellular Differentiation:

      Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.

      Interplay with Key Cytokines:

      Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.

      Therapeutic Implications and Tissue Regeneration:

      The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.

      Conclusion:

      As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 16.8kDa.

      What is the source or expression system of BMP7 Protein?
      Escherichia Coli.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The biological functionality of BMP7 Protein will be determined in the future.

      What is the amino acid sequence of BMP7 Protein?
      MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 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.

    Bmp 7 Human His