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Search results

1000 results found for “prefoldin”

Name

Description

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  • View Data Sheet

    Name :

    PSPN Human

    Description:

    Persephin Human Recombinant

    Persephin, PSP, PSPN.

    Product # :

    CYT-801

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    PSPN Human Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.5kDa. The PSPN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 10ng/ml, corresponding to a specific activity of > 1.0 × 100,000 IU/mg. 

    More Info

    • Introduction

      Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

    • Synonyms

      Persephin, PSP, PSPN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN in 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG.

    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.

    Pspn Human
  • View Data Sheet

    Name :

    HB-EGF Human

    Description:

    HB-EGF Human Recombinant

    HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    Product # :

    CYT-119

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • More Info

    Description

    HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

      KYVKELRAPS CICHPGYHGE RCHGLSL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.9kDa.

      What is the source or expression system of HB-EGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of HB-EGF Protein?
      The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
      KYVKELRAPS CICHPGYHGE RCHGLSL.

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

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-EGF 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.

    Hb Egf Human
  • View Data Sheet

    Name :

    ACVR2A Human

    Description:

    Actv Receptor Type 2A Human Recombinant

    ACVR2A, ACTRIIA, ACTR-IIA,

    Product # :

    CYT-976

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • sds-page

    Description

    ACVR2A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids (20-135a.a.) and having a molecular mass of 14.4kDa (Molecular size on SDS-PAGE will appear at approximately 28kDa.ACVR2A is fused to 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACVR2A protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    sds-page

    ACVR2A Human sds-page - Product image 1

    More Info

    • Introduction

      ACVR2A takes part in various biological processes including mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, carcinogenesis, and inflammation. ACVR2A which is a receptor for Actv A, Actv B and inhibin A mediates induction of adipogenesis by GDF6.

    • Synonyms

      ACVR2A, ACTRIIA, ACTR-IIA,

    • 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

      AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

    • Background

      A Comprehensive Examination of the Activin Receptor Type 2A Human Recombinant: Biological Functions and Therapeutic Possibilities

      1. Abstract

      This paper delves into the complex world of Activin Receptor Type 2A Human Recombinant (ACVR2A), a crucial element of the Transforming Growth Factor-beta (TGF-beta) signaling pathway. The structure, biological implications, and signaling pathway of ACVR2A are all extensively reviewed. The potential for ACVR2A as a therapeutic target in various pathological conditions is also explored.

      2. Introduction

      The ACVR2A, a receptor protein vital to the TGF-beta signaling pathway, plays a significant role in a multitude of biological processes, including embryogenesis, cell differentiation, and homeostasis. Understanding the intricate operations of ACVR2A could open the door to innovative therapeutic strategies.

      3. Structure and Signaling of ACVR2A

      As a transmembrane serine/threonine kinase receptor, ACVR2A is characterized by a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Upon binding of specific ligands like activin, ACVR2A interacts with type I receptors to trigger phosphorylation events, leading to the activation of downstream SMAD signaling pathways.

      4. Biological Functions of ACVR2A

      ACVR2A plays a substantial role in a wide range of biological processes. These include embryonic development, cell differentiation, bone growth, immune responses, and homeostasis. Furthermore, ACVR2A is instrumental in follicle-stimulating hormone (FSH) regulation, highlighting its importance in reproduction.

      5. ACVR2A in Disease Pathology

      Impairments in ACVR2A signaling have been linked to several diseases, including various cancers and reproductive disorders. Mutations in the ACVR2A gene have been implicated in tumor progression, underscoring the receptor's role in cell proliferation and differentiation.

      6. Therapeutic Potential of ACVR2A

      The centrality of ACVR2A in critical biological processes and disease pathology suggests its therapeutic potential. By modulating ACVR2A signaling, it may be possible to intervene in diseases characterized by aberrant TGF-beta signaling. Additionally, ACVR2A antagonists are being studied for their potential in cancer treatment.

      7. Conclusion and Future Perspectives

      Our comprehension of ACVR2A's functions has substantially increased in recent years, yet much remains to be discovered. Further research into ACVR2A's precise molecular mechanisms and involvement in disease will undoubtedly yield new therapeutic strategies.

      What is the molecular weight / Mw of ACVR2A Protein?
      ACVR2A Protein has a total Mw of 14.4kDa.
      What is the source or expression system of ACVR2A Protein?
      Sf9, Baculovirus cells.

      What is the Purity of ACVR2A Protein?
      ACVR2A Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ACVR2A Protein?
      The biological functionality of ACVR2A Protein will be determined in the future.

      What is the amino acid sequence of ACVR2A Protein?
      AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

      What applications can ACVR2A Protein be used in?
      ACVR2A Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ACVR2A Protein?
      The endotoxin level is minimal, ACVR2A 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.

    Acvr2A Human
  • View Data Sheet

    Name :

    CTSA Mouse

    Description:

    Cathepsin-A Mouse Recombinant

    Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    Product # :

    ENZ-945

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    Description

    CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect cells.

    Formulation

    CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.

    • Synonyms

      Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    • 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

      APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.

    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.

    Ctsa Mouse
  • View Data Sheet

    Name :

    AFAP1 Human

    Description:

    Actin Filament Associated Protein 1 Human Recombinant

    Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 1.

    Product # :

    PRO-1972

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    Description

    AFAP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 360 amino acids (250-588) and having a molecular mass of 39.2 kDa.AFAP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The AFAP1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin Filament Associated Protein 1 (AFAP1) is a Src binding partner. AFAP1 is a possible modulator of actin filament integrity in response to cellular signals, and is also playing a role as an adaptor protein by connecting Src family members to actin filaments. AFAP1 takes partin the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.

    • Synonyms

      Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 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

      MGSSHHHHHH SSGLVPRGSH MGCSGPVDSE CPPPPSSPVH KAELEKKLSS ERPSSDGEGV VENGITTCNG KEQVKRKKSS KSEAKGTVSK VTGKKITKII SLGKKKPSTD EQTSSAEEDV PTCGYLNVLS NSRWRERWCR VKDNKLIFHK DRTDLKTHIV SIPLRGCEVI PGLDCKHPLT FRLLRNGQEV AVLEASSSED MGRWIGILLA ETGSSTDPEA LHYDYIDVEM SASVIQTAKQ TFCFMNRRVI SANPYLGGTS NGYAHPSGTA LHYDDVPCIN GSLRGKKPPV ASNGVTGKGK TLSSQPKKAD PAAVVKRTGS NAAQYKYGKN RVEADAKRLQ TKEEELLKRK EALRNRLAQL.

    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.

    Afap1 Human
  • View Data Sheet

    Name :

    MSR1 Human, sf9

    Description:

    Macrophage Scavenger Receptor 1, sf9 Human Recombinant

    Macrophage Scavenger Receptor 1, Macrophage Acetylated LDL Receptor I And II, Scavenger Receptor Class A Member 1, SCARA1, Macrophage Scavenger Receptor Type III, CD204 Antigen, CD204, PhSR1, PhSR2, SR-A, SRA.

    Product # :

    PRO-2318

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    Description

    MSR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 384 amino acids (77-451 a.a.) and having a molecular mass of 42.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). MSR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MSR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Macrophage Scavenger Receptor 1, also known as MSR1 is a member of the class A macrophage scavenger receptors, which comprises three different types 1, 2 and 3 generated by alternative splicing. Furthermore, these receptors or isoforms are macrophage-specific trimeric integral membrane glycoproteins and have been implicated in many macrophage-associated physiological as well as pathological processes which include atherosclerosis, Alzheimer's disease, and host defense.

    • Synonyms

      Macrophage Scavenger Receptor 1, Macrophage Acetylated LDL Receptor I And II, Scavenger Receptor Class A Member 1, SCARA1, Macrophage Scavenger Receptor Type III, CD204 Antigen, CD204, PhSR1, PhSR2, SR-A, SRA.

    • 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

      ADPKWETKNC SVSSTNANDI TQSLTGKGND SEEEMRFQEV FMEHMSNMEK RIQHILDMEA NLMDTEHFQN FSMTTDQRFN DILLQLSTLF SSVQGHGNAI DEISKSLISL NTTLLDLQLN IENLNGKIQE NTFKQQEEIS KLEERVYNVS AEIMAMKEEQ VHLEQEIKGE VKVLNNITND LRLKDWEHSQ TLRNITLIQG PPGPPGEKGD RGPTGESGPR GFPGPIGPPG LKGDRGAIGF PGSRGLPGYA GRPGNSGPKG QKGEKGSGNT LTPFTKVRLV GGSGPHEGRV EILHSGQWGT ICDDRWEVRV GQVVCRSLGY PGVQAVHKAA HFGQGTGPIW LNEVFCFGRE SSIEECKIRQ WGTRACSHSE DAGVTCTLHH HHHH.

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    Msr1 Human Sf9
  • View Data Sheet

    Name :

    DCN Human

    Description:

    Decorin Human Recombinant

    Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    Product # :

    PRO-1583

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    Description

    DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

    • 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 MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.

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    Dcn Human
  • View Data Sheet

    Name :

    SERPING1 Human, Sf9

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant, Sf9

    Serpin Family G Member 1, Serpin Peptidase Inhibitor, Clade G (C1 Inhibitor), Member 1, Plasma Protease C1 Inhibitor, C1 Esterase Inhibitor, C1-Inhibiting Factor, Serpin G1, C1NH, C1IN, Serine (Or Cysteine) Proteinase Inhibitor, Clade G (C1 Inhibitor), Member 1, (Angioedema, Hereditary), Serine/Cysteine Proteinase Inhibitor Clade G Member 1, Serpin Peptidase Inhibitor Clade G Member 1, Complement Component 1 Inhibitor, Angioedema, Hereditary, C1 Inh, C1INH, C1Inh, HAE1, HAE2. 

    Product # :

    PRO-2589

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    Description

    SERPING1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (23-500a.a.) and having a molecular mass of 54.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SERPING1 is expressed with an 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPING1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 takes part in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. Lack of SERPING1 results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      Serpin Family G Member 1, Serpin Peptidase Inhibitor, Clade G (C1 Inhibitor), Member 1, Plasma Protease C1 Inhibitor, C1 Esterase Inhibitor, C1-Inhibiting Factor, Serpin G1, C1NH, C1IN, Serine (Or Cysteine) Proteinase Inhibitor, Clade G (C1 Inhibitor), Member 1, (Angioedema, Hereditary), Serine/Cysteine Proteinase Inhibitor Clade G Member 1, Serpin Peptidase Inhibitor Clade G Member 1, Complement Component 1 Inhibitor, Angioedema, Hereditary, C1 Inh, C1INH, C1Inh, HAE1, HAE2.

    • 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

      ADPEFNPNAT SSSSQDPESL QDRGEGKVAT TVISKMLFVE PILEVSSLPT TNSTTNSATK ITANTTDEPT TQPTTEPTTQ PTIQPTQPTT QLPTDSPTQP TTGSFCPGPV TLCSDLESHS TEAVLGDALV DFSLKLYHAF SAMKKVETNM AFSPFSIASL LTQVLLGAGE NTKTNLESIL SYPKDFTCVH QALKGFTTKG VTSVSQIFHS PDLAIRDTFV NASRTLYSSS PRVLSNNSDA NLELINTWVA KNTNNKISRL LDSLPSDTRL VLLNAIYLSA KWKTTFDPKK TRMEPFHFKN SVIKVPMMNS KKYPVAHFID QTLKAKVGQL QLSHNLSLVI LVPQNLKHRL EDMEQALSPS VFKAIMEKLE MSKFQPTLLT LPRIKVTTSQ DMLSIMEKLE FFDFSYDLNL CGLTEDPDLQ
      VSAMQHQTVL ELTETGVEAA AASAISVART LLVFEVQQPF LFVLWDQQHK FPVFMGRVYD PRAHHHHHH.

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    Serping1 Protein
  • View Data Sheet

    Name :

    DLK1 Human

    Description:

    Delta-Like 1 Human Recombinant

    DLK1, Delta-Like 1 Homolog (Drosophila), PREF1, DLK-1, FA1, DLK, PG2, Delta-Like Homolog (Drosophila), Protein Delta Homolog 1, Preadipocyte Factor 1, Fetal Antigen 1, Secredeltin, DELTA1, Pref-1, ZOG.

    Product # :

    PRO-2256

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    Description

    DLK1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303 a.a) and having a molecular mass of 30.7kDa.DLK1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DLK1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Delta-Like 1, also known as DLK1 is a member of the Notch/Delta/Serrate family of epidermal growth factor (EGF)-like repeat-containing proteins which act as ligands in the Notch signaling pathway. Furthermore, DLK1 has six highly conserved epidermal-growth-factor motifs and it also contains up to ten O-glycosylation and N-glycosylation locations, six of them are differentially glycosylated.

    • Synonyms

      DLK1, Delta-Like 1 Homolog (Drosophila), PREF1, DLK-1, FA1, DLK, PG2, Delta-Like Homolog (Drosophila), Protein Delta Homolog 1, Preadipocyte Factor 1, Fetal Antigen 1, Secredeltin, DELTA1, Pref-1, ZOG.

    • 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

      AECFPACNPQ NGFCEDDNVC RCQPGWQGPL CDQCVTSPGC LHGLCGEPGQ CICTDGWDGE LCDRDVRACS SAPCANNGTC VSLDDGLYEC SCAPGYSGKD CQKKDGPCVI NGSPCQHGGT CVDDEGRASH ASCLCPPGFS GNFCEIVANS CTPNPCENDG VCTDIGGDFR CRCPAGFIDK TCSRPVTNCA SSPCQNGGTC LQHTQVSYEC LCKPEFTGLT CVKKRALSPQ QVTRLPSGYG LAYRLTPGVH ELPVQQPEHR ILKVSMKELN KKTPLLTEGQ LEHHHHHH.

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    Dlk1 Human
  • View Data Sheet

    Name :

    NECTIN2 Human

    Description:

    Nectin Cell Adhesion Molecule 2 Human Recombinant

    Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.

    Product # :

    PRO-2461

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    Description

    NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NECTIN2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.

    • Synonyms

      Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.

    • 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

      QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.

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    Nectin2 Human
  • View Data Sheet

    Name :

    EFNA1 Human, HEK

    Description:

    Ephrin A1 Human Recombinant, HEK

    Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    Product # :

    PRO-2477

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    Description

    EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    • 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 one week 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. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS HHHHHH.

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    Efna1 Protein
  • View Data Sheet

    Name :

    SNTA1 Human

    Description:

    Syntrophin, Alpha 1 Human Recombinant

    Alpha-1-syntrophin, 59 kDa dystrophin-associated protein A1 acidic component 1, Pro-TGF-alpha cytoplasmic domain-interacting protein 1, TACIP1, Syntrophin-1, SNTA1, SNT1, LQT12, dJ1187J4.5.

    Product # :

    PRO-1016

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    Description

    SNTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (1-505 a.a.) and having a molecular mass of 56.3kDa. SNTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SNTA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNTA1 is a member of the syntrophin gene family. SNTA1 is a peripheral membrane protein found linked with dystrophin and dystrophin-related proteins. Dystrophin is a large, rod-like cytoskeletal protein located at the inner surface of muscle fibers. Dystrophin is absent in Duchenne Muscular Dystrophy patients, however it is present in reduced amounts in Becker Muscular Dystrophy patients. Syntrophins are cytoplasmic peripheral membrane scaffold proteins and components of the dystrophin-associated protein complex. The N-terminal PDZ domain of SNTA1 interacts with the C-terminus of the pore-forming alpha subunit (SCN5A) of the cardiac sodium channel Nav1.5. In addition, SNTA1 associates cardiac sodium channels with the nitric oxide synthase-PMCA4b (plasma membrane Ca-ATPase subtype 4b) complex in cardiomyocytes. The SNTA1 gene is a predisposition locus for Long-QT syndrome (LQT) - an inherited disorder associated with sudden cardiac death from arrhythmia - and sudden infant death syndrome (SIDS). SNTA1 also associates with dystrophin and dystrophin-related proteins at the neuromuscular junction and modifies intracellular calcium ion levels in muscle tissue.

    • Synonyms

      Alpha-1-syntrophin, 59 kDa dystrophin-associated protein A1 acidic component 1, Pro-TGF-alpha cytoplasmic domain-interacting protein 1, TACIP1, Syntrophin-1, SNTA1, SNT1, LQT12, dJ1187J4.5.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMASGRRA PRTGLLELRA GAGSGAGGER WQRVLLSLAE DVLTVSPADG DPGPEPGAPR EQEPAQLNGA AEPGAGPPQL PEALLLQRRR VTVRKADAGG LGISIKGGRE NKMPILISKI FKGLAADQTE ALFVGDAILS VNGEDLSSAT HDEAVQVLKK TGKEVVLEVK YMKDVSPYFK NSTGGTSVGW DSPPASPLQR QPSSPGPTPR NFSEAKHMSL KMAYVSKRCT PNDPEPRYLE ICSADGQDTL FLRAKDEASA RSWATAIQAQ VNTLTPRVKD ELQALLAATS TAGSQDIKQI GWLTEQLPSG GTAPTLALLT EKELLLYLSL PETREALSRP ARTAPLIATR LVHSGPSKGS VPYDAELSFA LRTGTRHGVD THLFSVESPQ ELAAWTRQLV DGCHRAAEGV QEVSTACTWN GRPCSLSVHI DKGFTLWAAE PGAARAVLLR QPFEKLQMSS DDGASLLFLD FGGAEGEIQL DLHSCPKTIV FIIHSFLSAK VTRLGLLA.

    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.

    Snta1 Human
  • View Data Sheet

    Name :

    EFNB1 Human, Sf9

    Description:

    Ephrin-B1 Human Recombinant, Sf9

    Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2. 

    Product # :

    PRO-2543

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    Description

    EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

    • Synonyms

      Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 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

      ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
      SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
      QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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

    Ephrin B1
  • View Data Sheet

    Name :

    SRSF1 Human, Sf9

    Description:

    Serine/arginine-Rich Splicing Factor 1 Human Recombinant, Sf9

    SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.

    Product # :

    PRO-2417

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    Description

    SRSF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (1-248) and having a molecular mass of 28.5kDa. SRSF1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SRSF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 100mM KCl, 1mM DTT, 0.2mM EDTA and 40% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.

    • Synonyms

      SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 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

      MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH 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.

    Srsf1 Human Sf9
  • View Data Sheet

    Name :

    C1QTNF3 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 3 Human Recombinant

    Complement C1q tumor necrosis factor-related protein 3, Secretory protein CORS26, C1QTNF3, CTRP3, Cors, Corcs, CORS26, FLJ37576, Cartducin.

    Product # :

    PRO-653

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    Description

    C1QTNF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 234 amino acids and having a molecular mass of 25.4 kDa. The protein contains an extra 10 aa His tag at N-terminus. The C1QTNF3 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ4 amino acids 23–246. The C1QTNF3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human C1QTNF3 was filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M Acetate buffer pH4.

    Purity

    The purity of C1QTNF3 is greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      C1QTNF3 also called Cartducin is a novel angiogenic factor in the formation of neointima following angioplasty. C1QTNF3 a paralog of Acrp30 (adiponectin). C1QTNF3 is a secretory protein produced by chondrogenic precursors & proliferating chondrocytes, and belongs to a novel C1q family of proteins. Cartducin promotes the growth of mesenchymal chondroprogenitor cells & chondrosarcoma-derived chondrocytic cells in vitro. Cartducin stimulates mesenchymal chondroprogenitor cell proliferation through extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways. C1QTNF3 promotes proliferation & the migration of endothelial cells.

    • Synonyms

      Complement C1q tumor necrosis factor-related protein 3, Secretory protein CORS26, C1QTNF3, CTRP3, Cors, Corcs, CORS26, FLJ37576, Cartducin.

    • Stability

      Store lyophilized C1QTNF3 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF3 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of the protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS QDEYMESPQT GGLPPDCSKC CHGDYSFRGY QGPPGPPGPP GIPGNHGNNG NNGATGHEGA KGEKGDKGDL GPRGERGQHG PKGEKGYPGI PPELQIAFMA SLATHFSNQN SGIIFSSVET NIGNFFDVMT GRFGAPVSGV YFFTFSMMKH EDVEEVYVYL MHNGNTVFSM YSYEMKGKSD TSSNHAVLKL AKGDEVWLRM GNGALHGDHQ RFSTFAGFLLFETK.

    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.

    C1Qtnf3 Human
  • View Data Sheet

    Name :

    PIN1 Mouse

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.

    Product # :

    ENZ-1045

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    Description

    PIN1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.8kDa. PIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,200 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.

    • 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 MGSMADEEKL PPGWEKRMSR SSGRVYYFNH ITNASQWERP SGGSTVGGSS KNGQGEPAKV RCSHLLVKHS QSRRPSSWRQ EKITRSKEEA LELINGYIQK IKSGEEDFES LASQFSDCSS AKARGDLGPF SRGQMQKPFE DASFALRTGE MSGPVFTDSG IHIILRTE.

    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.

    Pin1 Mouse
  • View Data Sheet

    Name :

    PRKAG1 Human

    Description:

    Protein Kinase, AMP-Activated, Gamma 1 Human Recombinant

    Protein Kinase AMP-Activated Gamma 1 Non-Catalytic Subunit, 5'-AMP-Activated Protein Kinase Subunit Gamma-1, AMPK Gamma1 Chain, AMPKg.

    Product # :

    PKA-305

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    Description

    PRKAG1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-331) and having a molecular mass of 40.0kDa.PRKAG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRKAG1 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

      PRKAG1 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme which supervises cellular energy status. PRKAG1 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding dissimilar isoforms were found.

    • Synonyms

      Protein Kinase AMP-Activated Gamma 1 Non-Catalytic Subunit, 5'-AMP-Activated Protein Kinase Subunit Gamma-1, AMPK Gamma1 Chain, AMPKg.

    • 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 MGSMETVISS DSSPAVENEH PQETPESNNS VYTSFMKSHR CYDLIPTSSK LVVFDTSLQV KKAFFALVTN GVRAAPLWDS KKQSFVGMLT ITDFINILHR YYKSALVQIY ELEEHKIETW REVYLQDSFK PLVCISPNAS LFDAVSSLIR NKIHRLPVID PESGNTLYIL THKRILKFLK LFITEFPKPE FMSKSLEELQ IGTYANIAMV RTTTPVYVAL GIFVQHRVSA LPVVDEKGRV VDIYSKFDVI NLAAEKTYNN LDVSVTKALQ HRSHYFEGVL KCYLHETLET IINRLVEAEV HRLVVVDEND VVKGIVSLSD ILQALVLTGG EKKP

    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.

    Prkag1 Human
  • View Data Sheet

    Name :

    Procalcitonin Human

    Description:

    Procalcitonin Human Recombinant

    Procalcitonin, PCT.

    Product # :

    HOR-304

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    Description

    Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 10mM sodium phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Procalcitonin, PCT.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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 procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.

    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.

    Procalcitonin Human
  • View Data Sheet

    Name :

    GLYATL2 Human

    Description:

    Glycine-N-Acyltransferase-Like 2 Human Recombinant

    BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    Product # :

    ENZ-770

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    Description

    GLYATL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-294a.a) and having a molecular mass of 36.7kDa. GLYATL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLYATL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.

    • Synonyms

      BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    • 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 MGSMLVLHNS QKLQILYKSL EKSIPESIKV YGAIFNIKDK NPFNMEVLVD AWPDYQIVIT RPQKQEMKDD QDHYTNTYHI FTKAPDKLEE VLSYSNVISW EQTLQIQGCQ EGLDEAIRKV ATSKSVQVDY MKTILFIPEL PKKHKTSSND KMELFEVDDD NKEGNFSNMF LDASHAGLVN EHWAFGKNER SLKYIERCLQ DFLGFGVLGP EGQLVSWIVM EQSCELRMGY TVPKYRHQGN MLQIGYHLEK YLSQKEIPFY FHVADNNEKS LQALNNLGFK ICPCGWHQWK CTPKKYC.

    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.

    Glyatl2 Human
  • View Data Sheet

    Name :

    GNMT Human, Active

    Description:

    Glycine N-Methyltransferase Human Recombinant , Active

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

    Product # :

    ENZ-1059

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Gnmt Human Active
  • View Data Sheet

    Name :

    GSTO2 Human

    Description:

    Glutathione S-Transferase Omega 2 Human Recombinant

    Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.

    Product # :

    ENZ-605

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    Description

    GSTO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243) and having a molecular mass of 30.6kDa.GSTO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily. GSTO2 is involved in catalyzing the reaction of glutathione with a broad range of organic compounds to form thioethers, a process which is vital for the metabolism and detoxification of a variety of xenobiotics and carcinogens. GSTO2 displays glutathione-dependent thiol transferase activity. GSTO2 has a high dehydroascorbate reductase activity and may be a factor in the recycling of ascorbic acid. GSTO2 also participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). GSTO2 is expressed in an array of tissues, including the liver, kidney, skeletal muscle and prostate, while the strongest expression is seen in the testis.

    • Synonyms

      Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.

    • 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 MGSMSGDATR TLGKGSQPPG PVPEGLIRIY SMRFCPYSHR TRLVLKAKDI RHEVVNINLR NKPEWYYTKH PFGHIPVLET SQCQLIYESV IACEYLDDAY PGRKLFPYDP YERARQKMLL ELFCKVPHLT KECLVALRCG RECTNLKAAL RQEFSNLEEI
      LEYQNTTFFG GTCISMIDYL LWPWFERLDV YGILDCVSHT PALRLWISAM KWDPTVCALL MDKSIFQGFL NLYFQNNPNA FDFGLC.

    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.

    Gsto2 Human
  • View Data Sheet

    Name :

    AOD-9604

    Description:

    AOD-9604

    Product # :

    HOR-064

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • formulation
    • purity
    • More Info

    Description

    AOD-9604 is a synthetic single, non-glycosylated polypeptide chain containing 16 amino acids, having a molecular mass of 1815 Dalton and a Molecular formula of C78H123N23O23 S2.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized AOD-9604 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AOD-9604 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 AOD-9604 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-SerVal-Glu-Gly-Ser-Cys-Gly-Phe-OH (Disulfide bond).

    • Background

      AOD-9604 is a synthetic analog of the C-terminal fragment (177–191) AOD-9604 stimulates lipolysis (fat breakdown) without the unwanted growth-promoting or insulin-antagonizing effects of full-length hGH. AOD-9604 is a potent lipolytic tool in animal models and researchers focus on its regenerative properties in joint health and its ability to modulate beta3 adrenergic receptors without the systemic risks of growth hormone.

    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.

    AOD-9604
  • View Data Sheet

    Name :

    Cyclophilin B Antibody

    Description:

    Cyclophilin-B, Mouse Anti Human

    Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.

    Product # :

    ANT-380

    Price :

    Quantity :

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    Shipped with Ice Packs

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    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

    • Synonyms

      Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.

    • Immunogen

      Anti-human Cyclophilin-B mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cyclophilin-B amino acids 26-216 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      Pk2E2AT.

    • Applications

      Cyclophilin-B 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.

    • 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

      Cyclophilin-B 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.

    Cyclophilin B Antibody
  • View Data Sheet

    Name :

    Histrelin

    Description:

    Histrelin

    Product # :

    HOR-244

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • formulation
    • purity
    • More Info

    Description

    Histrelin has a molecular formula of C66H86N18O12, a.a. sequence of Pyr-His-Trp-Ser-Tyr-D-His(Bzl)-Leu-Arg-Pro-NHEt and having a Mw of 1323.32 Dalton.

    Formulation

    The Histrelin peptide was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Histrelin is a hormone similar to one normally released from the hypothalamus gland in the brain. Histrelin works by decreasing the amount of estrogen and testosterone in the blood. Suppressing estrogen can cause thinning of the bones or slowing of their growth. Histrelin acetate is a potent LHRH agonist which stimulates LH and FSH release and inhibits the actions of sex steroids on the male and female reproductive tracts. After a transient increase, continuous administration results in down regulation of LH and FSH levels followed by a suppression of ovarian and testicular steroid biosynthesis. Histrelin potency in vivo and in vitro is similar to that of the D-Trp6-containing analog. Especially because of its high water solubility and greater lipophilic character, it appears promising for clinical application.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Histrelin
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