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Search results

1000 results found for “Fibronectin”

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  • View Data Sheet

    Name :

    ING2 Human

    Description:

    Inhibitor of Growth Family, Member 2 Human Recombinant

    Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    Product # :

    PRO-1739

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    Description

    ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).

    • Synonyms

      Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    • 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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.

    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.

    Ing2 Human
  • View Data Sheet

    Name :

    MBP Human

    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

    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.

    Mbp Protein
  • View Data Sheet

    Name :

    MBP Protein

    Description:

    Myelin Basic Protein Human

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2798

    Price :

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    Description

    MBP Human produced in Human brain is checked using poly and monoclonal antibodies against MBP.

    Source

    Human brain.

    Formulation

    MBP was lyophilized containing no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Myelin Basic Protein (MBP) stands as a cornerstone in the intricate architecture of the nervous system. As a vital component of the myelin sheath, MBP plays a pivotal role in ensuring the integrity and rapid transmission of nerve impulses. Over the years, scientific inquiry into MBP has revealed its multifaceted functions, not only as a structural element but also as a regulatory molecule involved in various cellular processes. This research seeks to unravel the complexities of MBP, exploring its structural characteristics, physiological significance, and its involvement in neurological disorders.

      Structural Marvel of MBP:

      MBP, an intrinsically disordered protein, boasts a unique structure allowing it to interact with lipid membranes, especially those found in the myelin sheath. Its high arginine and lysine content gives it a positive charge, enabling strong electrostatic interactions with the negatively charged lipids in myelin. This structural adaptation is crucial for the compact wrapping of myelin around axons, facilitating efficient electrical signal conduction.

      Physiological Significance in Myelination:

      In the central nervous system (CNS), oligodendrocytes produce myelin, a lipid-rich substance that insulates axons. MBP, as a major constituent of myelin, plays an indispensable role in this process. It stabilizes the myelin sheath’s structure, ensuring its tight adherence to the axon and promoting the fast, saltatory conduction of nerve impulses. Without functional MBP, myelin integrity is compromised, leading to reduced nerve conduction velocity and impaired neural communication.

      Beyond Structural Functions:

      Recent studies have revealed that MBP is not merely a structural protein but also possesses regulatory functions. It participates in signaling pathways crucial for oligodendrocyte development and myelination. Moreover, MBP’s interaction with cytoskeletal elements suggests its involvement in cellular processes such as axon guidance and neuronal plasticity. Understanding these regulatory roles provides insights into the broader impact of MBP on neural development and function.

      Implications in Neurological Disorders:

      Alterations in MBP have been linked to various neurological disorders, including multiple sclerosis (MS). In MS, the immune system erroneously targets MBP, leading to demyelination and subsequent neurological impairments. Research into MBP-related pathologies not only aids in understanding disease mechanisms but also offers potential therapeutic avenues. Targeting MBP-specific immune responses is a focus of research for developing MS treatments.

      Conclusion:

      MBP, as the guardian of neural transmission, stands as a testament to the marvels of biological architecture. Its intricate structure and multifaceted functions make it indispensable for the proper functioning of the nervous system. Beyond its role as a structural protein, MBP’s involvement in cellular signalling adds layers to its significance. In the realm of neurological disorders, MBP’s complexities provide both challenges and opportunities, guiding scientists toward innovative therapies. This research delves into the world of MBP, appreciating its contributions to neuroscience while aiming to decipher the mysteries that lie within its molecular intricacies.

    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.

    Mbp Human
  • View Data Sheet

    Name :

    S100A11 Human

    Description:

    S100 Calcium Binding Protein A11 Human Recombinant

    Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

    Product # :

    PRO-385

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    Description

    S100A11 Human Recombinant is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.

    Source

    Escherichia Coli.

    Formulation

    S100A11 is supplied in PBS and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    2 bands on Western blot at 17 and 34 kDa, respectively representing monomeric and dimeric form.

    More Info

    • Introduction

      S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. 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 S100A11 have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      S100A11 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    S100A11 Human
  • View Data Sheet

    Name :

    Adipsin Human, Sf9

    Description:

    Complement Factor D Human Recombinant, Sf9

    Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    Product # :

    PRO-2213

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    Description

    Adipsin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 241 amino acids (21-253a.a.) and having a molecular mass of 26.01kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). Adipsin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Adipsin protein solution (1mg/ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

    • Synonyms

      Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    • 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

      PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLAVEHHHHH H.

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    Adipsin Human Sf9
  • View Data Sheet

    Name :

    CUEDC1 Human

    Description:

    CUE Domain Containing 1 Human Recombinant

    CUE Domain Containing 1, CUE Domain-Containing Protein 1.

    Product # :

    PRO-1822

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    Description

    CUEDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 44.6kDa.CUEDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CUEDC1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 1, also know as CUEDC1 contains 1 CUE domain. The CUE domain is structurally associated to the ubiquitin-binding UBA domain and exists as a domain-swapped dimer which makes additional contacts with ubiquitin, and as a result, binds ubiquitin with higher affinity. The CUE domain is discovered in proteins with diverse functions including protein sorting and degradation of misfolded proteins in the endoplasmic reticulum.

    • Synonyms

      CUE Domain Containing 1, CUE Domain-Containing Protein 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTSLFRR SSSGSGGGGT AGARGGGGGT AAPQELNNSR PARQVRRLEF NQAMDDFKTM FPNMDYDIIE CVLRANSGAV DATIDQLLQM NLEGGGSSGG VYEDSSDSED SIPPEILERT LEPDSSDEEP PPVYSPPAYH MHVFDRPYPL APPTPPPRID ALGSGAPTSQ RRYRNWNPPL LGNLPDDFLR ILPQQLDSIQ GNAGGPKPGS GEGCPPAMAG PGPGDQESRW KQYLEDERIA LFLQNEEFMK ELQRNRDFLL ALERDRLKYE SQKSKSSSVA VGNDFGFSSP VPGTGDANPA VSEDALFRDK LKHMGKSTRR KLFELARAFS EKTKMRKSKR KHLLKHQSLG AAASTANLLD DVEGHACDED FRGRRQEAPK VEEGLREGQ

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    Cuedc1 Human
  • View Data Sheet

    Name :

    MMP9 Human, Sf9

    Description:

    Matrix Metalloproteinase-9 Human Recombinant, Sf9

    Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    Product # :

    ENZ-1091

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    Description

    MMP9 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a.) and having a molecular mass of 77.1 kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP9 protein solution ( 0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

    • Synonyms

      Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    • 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

      APRQRQSTLV LFPGDLRTNL TDRQLAEEYL YRYGYTRVAE MRGESKSLGP ALLLLQKQLS LPETGELDSA TLKAMRTPRC GVPDLGRFQTFEGDLKWHHH NITYWIQNYS EDLPRAVIDD AFARAFALWS AVTPLTFTRV YSRDADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGVVVP TRFGNADGAA CHFPFIFEGR SYSACTTDGR SDGLPWCSTT ANYDTDDRFG FCPSERLYTQ DGNADGKPCQ FPFIFQGQSY SACTTDGRSD GYRWCATTAN YDRDKLFGFC PTRADSTVMG GNSAGELCVF PFTFLGKEYS TCTSEGRGDG RLWCATTSNF DSDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPMYRFTEGP PLHKDDVNGI RHLYGPRPEP EPRPPTTTTP QPTAPPTVCP TGPPTVHPSE RPTAGPTGPP SAGPTGPPTA GPSTATTVPL SPVDDACNVN IFDAIAEIGN QLYLFKDGKY WRFSEGRGSR PQGPFLIADK WPALPRKLDS VFEERLSKKL FFFSGRQVWV YTGASVLGPR RLDKLGLGAD VAQVTGALRS GRGKMLLFSG RRLWRFDVKA QMVDPRSASE VDRMFPGVPL DTHDVFQYRE KAYFCQDRFY WRVSSRSELN QVDQVGYVTY DILQCPEDHH HHHH.

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    Mmp9 Enzyme
  • View Data Sheet

    Name :

    SCGB2A2 Human, HEK

    Description:

    Mammaglobin-A Human Recombinant, HEK

    Mammaglobin-A, Mammaglobin-1, Secretoglobin family 2A member 2, SCGB2A2, MGB1, UGB2, MGC71974.

    Product # :

    PRO-2038

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    Description

    Mammaglobin-A Human Recombinant (Fc Chimera) produced in HEK cells is a single, glycosylated, polypeptide chain (Gly19-Phe93) containing a total of 321 amino acids, having a calculated molecular mass of 36.3kDa. The SCGB2A2 protein is fused to a 2 aa C-terminal linker, a 6 aa C-terminal His tag, a 7 aa TEV site and a 231 aa Human IgG1 fragment (Pro100-Lys330).

    Source

    HEK 293.

    Formulation

    SCGB2A2 was filtered (0,4µm) and lyophilized from 0.5mg/ml in PBS buffer and 5% (w/v) Threalose pH 7.4

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The mammaglobin gene was first identified using a differential screening approach directed at the isolation of novel, human breast cancer-associated genes. Mammaglobin encodes a 10 kDa glycoprotein and is distantly relaetd to a family of epithelial secretory proteins that includes rat estramustine-binding protein/prostatein and human Clara cell 10 kDa protein (CC10)/uteroglobin. Mammaglobin, a mammary-specific member of the uterglobin family, is known to be overexpressed in human breast cancer. Studies suggest that mammaglobin is one of the first relatively mammary-specific and mammary-sensitive markers (85%). Mammaglobin may be valuable used in a panel with BRST-2 (GCDFP-15) and ER in evaluating tumors of unknown primary sites.
      SCGB2A2 (the mammaglobin gene) is located on chromosome 11, at locus 11q13. SCGB2A2 is member of the secretoglobin superfamily of which is a group of small dimeric secreted and sometimes glycosylated proteins. Expressed mainly in mucosa, secretoglobins appear to be involved in cell signalling, immune response, chemotaxis, and might also serve as transporters for steroid hormones in humans.

    • Synonyms

      Mammaglobin-A, Mammaglobin-1, Secretoglobin family 2A member 2, SCGB2A2, MGB1, UGB2, MGC71974.

    • Physical Appearance

      Sterile filtered lyophilized 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 5 days.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      GSGCPLLENV ISKTINPQVS KTEYKELLQE FIDDNATTNA IDELKECFLN QTDETLSNVE VFMQLIYDSS LCDLF KLENL YFQGPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

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    Scgb2A2 Human Hek
  • View Data Sheet

    Name :

    SERPINB2 Human

    Description:

    Serpin Peptidase Inhibitor, Clade B Member 2 Human Recombinant

    Serpin Peptidase Inhibitor Clade B (Ovalbumin) Member 2, Serine (Or Cysteine) Proteinase Inhibitor Clade B (Ovalbumin) Member 2, Placental Plasminogen Activator Inhibitor, Plasminogen Activator Inhibitor Type II (Arginine-Serpin), PAI2, PLANH2, Monocyte Arg-Serpin, Serpin B2, HsT1201, PAI.

    Product # :

    PRO-1788

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    Description

    SERPINB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids and having a molecular mass of 46.6kDa.The SERPINB2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH8.0, 150mM NaCl, 1mM Cysteine, with 5% Trehalose.

    Purity

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

    Biological Activity

    The biologically active was determined by its inhibitory effect against single chain tPA induced cleavage of a chromogenic substrate in Imidazole Buffer at 37°C. Half maximal inhibition against 1.0 µg/ml of single chain tPA was at a concentration of 1.0µg/ml. 

    More Info

    • Introduction

      SERPINB2 is an inhibitory serpin produced primarily in keratinocytes, stimulated monocytes, and placental trophoblasts. SERPINB2 is found primarily as a 47 kDa non-glycosylated intracellular protein that is induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated SERPINB2 are similarly effective as inhibitors of uPA, the only proven physiological target of SERPINB2.

    • Synonyms

      Serpin Peptidase Inhibitor Clade B (Ovalbumin) Member 2, Serine (Or Cysteine) Proteinase Inhibitor Clade B (Ovalbumin) Member 2, Placental Plasminogen Activator Inhibitor, Plasminogen Activator Inhibitor Type II (Arginine-Serpin), PAI2, PLANH2, Monocyte Arg-Serpin, Serpin B2, HsT1201, PAI.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINB2 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 SERPINB2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEDLCVANTL FALNLFKHLA KASPTQNLFL SPWSISSTMA MVYMGSRGST EDQMAKVLQF NEVGANAVTP MTPENFTSCG FMQQIQKGSY PDAILQAQAA DKIHSSFRSL SSAINASTGN YLLESVNKLF GEKSASFREE YIRLCQKYYS SEPQAVDFLE CAEEARKKIN SWVKTQTKGK IPNLLPEGSV DGDTRMVLVN AVYFKGKWKT PFEKKLNGLY PFRVNSAQRT PVQMMYLREK LNIGYIEDLK AQILELPYAG DVSMFLLLPD EIADVSTGLE LLESEITYDK LNKWTSKDKM AEDEVEVYIP QFKLEEHYEL RSILRSMGME DAFNKGRANF SGMSERNDLF LSEVFHQAMV DVNEEGTEAA AGTGGVMTGR TGHGGPQFVA DHPFLFLIMH KITNCILFFG RFSSP

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    Serpinb2 Human
  • View Data Sheet

    Name :

    SERPINF2 Mouse

    Description:

    Serpin Peptidase Inhibitor, Clade F Member 2 Mouse Recombinant

    Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.

    Product # :

    PRO-2240

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    Description

    SERPINF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 470 amino acids (28-491 a.a.) and having a molecular mass of 52.9kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). SERPINF2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINF2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha-2-antiplasmin (SERPINF2) is a serine protease inhibitor. The main targets of SERPINF2 are plasmin and trypsin; however SERPINF2 also inactivates matriptase-3/TMPRSS7 and chymotrypsin.

    • Synonyms

      Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.

    • 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

      VDLPGQQPVS EQAQQKLPLP ALFKLDNQDF GDHATLKRSP GHCKSVPTAE ETRRLAQAMM AFTTDLFSLV AQTSTSSNLV LSPLSVALAL SHLALGAQNQ TLHSLHRVLH MNTGSCLPHL LSHFYQNLGP GTIRLAARIY LQKGFPIKDD FLEQSERLFG AKPVKLTGKQ EEDLANINQW VKEATEGKIE DFLSELPDST VLLLLNAIHF HGFWRTKFDP SLTQKDFFHL DERFTVSVDM MHAVSYPLRW FLLEQPEIQV AHFPFKNNMS FVVVMPTYFE WNVSEVLANL TWDTLYHPSL QERPTKVWLP KLHLQQQLDL VATLSQLGLQ ELFQGPDLRG ISEQNLVVSS VQHQSTMELS EAGVEAAAAT SVAMNRMSLS SFTVNRPFLF FIMEDTIGVP LFVGSVRNPN PSALPQLQEQ RDSPDNRLIG QNDKADFHGG KTFGPDLKLA PRMEEDYPQF SSPKHHHHHH.

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    Serpinf2 Mouse
  • View Data Sheet

    Name :

    NDRG3 Human

    Description:

    N-Myc Downstream Regulated 3 Human Recombinant

    Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.

    Product # :

    PRO-2100

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    Description

    NDRG3 Human Recombinant produced in E. coli is a single polypeptide chain containing 386 amino acids (1-363) and having a molecular mass of 42.4 kDa.NDRG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NDRG3 solution (0.25mg/1ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.

    • Synonyms

      Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.

    • 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 MGSMDELQDV QLTEIKPLLN DKEHDIETTH GVVHVTIRGL PKGNRPVILT YHDIGLNHKS CFNAFFNFED MQEITQHFAV CHVDAPGQQE GAPSFPTGYQ YPTMDELAEM LPPVLTHLSL KSIIGIGVGA GAYILSRFAL NHPELVEGLV LINVDPCAKG WIDWAASKLS GLTTNVVDII LAHHFGQEEL QANLDLIQTY RMHIAQDINQ DNLQLFLNSY NGRRDLEIER PILGQNDNKS KTLKCSTLLV VGDNSPAVEA VVECNSRLNP INTTLLKMAD CGGLPQVVQP GKLTEAFKYF LQGMGYIPSA SMTRLARSRT HSTSSSLGSG ESPFSRSVTS NQSDGTQESC ESPDVLDRHQ TMEVSC.

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    Ndrg3 Human
  • View Data Sheet

    Name :

    DRG1 Human

    Description:

    Developmentally Regulated GTP Binding Protein 1 Human Recombinant

    Developmentally-regulated GTP-binding protein 1, DRG-1, Neural precursor cell expressed developmentally down-regulated protein 3, NEDD-3, DRG1, NEDD3.

    Product # :

    PRO-885

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    Description

    DRG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 42.7kDa.DRG1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DRG1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 1mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Developmentally-regulated GTP-binding protein 1 (DRG1) is a member of the GTP1/OBG family. DRG1 has a role in cell proliferation and differentiation, as well as in apoptosis, proposing a role in tumor formation and metastasis. Expression of the DRG1 was considerably reduced in breast tumor cells, particularly in patients with lymph node or bone metastasis as compared to those with localized breast cancer. The DRG1 protein is expressed at high levels in the heart, kidney and skeletal muscle and at lower levels in the brain, liver, placenta, lung, colon and spleen.

    • Synonyms

      Developmentally-regulated GTP-binding protein 1, DRG-1, Neural precursor cell expressed developmentally down-regulated protein 3, NEDD-3, DRG1, NEDD3.

    • 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 MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVIRYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNSKPPNIG FKKKDKGGIN LTATCPQSEL DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV GKDHTLEDED VIQIVKK.

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    Drg1 Human
  • View Data Sheet

    Name :

    Noggin Human, Sf9

    Description:

    Noggin Human Recombinant, Sf9

    SYM1, SYNS1, NOG.

    Product # :

    CYT-1119

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    Description

    Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.

    Purity

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

    Biological Activity

    Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.

    More Info

    • Introduction

      Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.

    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.

    Noggin Protein
  • View Data Sheet

    Name :

    BCCIP Human

    Description:

    BRCA2 And CDKN1A Interacting Protein Human Recombinant

    BRCA2 and CDKN1A-interacting protein, P21- and CDK-associated protein 1, Protein TOK-1, BCCIP, TOK1, BRCA2 and CDKN1A-interacting protein.

    Product # :

    PRO-2014

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    Description

    BCCIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-314 a.a.) and having a molecular mass of 38.6kDa.BCCIP is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCCIP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BRCA2 And CDKN1A Interacting Protein (BCCIP) is a nuclear protein with multiple interacting domains which remained conserved throughout the evolution. BCCIP is an important cofactor for BRCA2 in tumor suppression, and a modulator of CDK2 kinase activity via p21. BCCIP takes also part in the regulation of BRCA2 and RAD51 nuclear focus formation, doublestrand break-induced homologous recombination, and cell cycle progression.

    • Synonyms

      BRCA2 and CDKN1A-interacting protein, P21- and CDK-associated protein 1, Protein TOK-1, BCCIP, TOK1, BRCA2 and CDKN1A-interacting protein.

    • 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 MGSEFMASRS KRRAVESGVP QPPDPPVQRD EEEEKEVENE DEDDDDSDKE KDEEDEVIDE EVNIEFEAYS LSDNDYDGIK KLLQQLFLKA PVNTAELTDL LIQQNHIGSV IKQTDVSEDS NDDMDEDEVF GFISLLNLTE RKGTQCVEQI QELVLRFCEK NCEKSMVEQL DKFLNDTTKP VGLLLSERFI NVPPQIALPM YQQLQKELAG AHRTNKPCGK CYFYLLISKT FVEAGKNNSK KKPSNKKKAA LMFANAEEEF FYEKAILKFN YSVQEESDTC LGGKWSFDDV PMTPLRTVML IPGDKMNEIM DKLKEYLSV.

    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.

    Bccip Human
  • View Data Sheet

    Name :

    ESM1 Human, HEK

    Description:

    Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK

    Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan. 

    Product # :

    PRO-2476

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    Description

    ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.

    • Synonyms

      Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ESM1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH HHHHH.

    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.

    Esm1 Protein
  • View Data Sheet

    Name :

    ILK1 Human

    Description:

    Integrin Linked Kinase Human Recombinant

    Integrin-linked protein kinase, ILK-1, ILK-2, 59 kDa serine/threonine-protein kinase, p59ILK, ILK, ILK1, ILK2, DKFZp686F1765, P59.

    Product # :

    PKA-353

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    Description

    ILK1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 452 amino acids fragment (1-452) having a molecular mass of 55.92kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The ILK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ILK1 protein is supplied in 25mM Sodium Acetate (pH 4.8) and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ILK1 (Integrin-linked kinase) is a serine/threonine protein kinase, containing 4 ankyrin-like repeats. ILK1 regulates a number of biological properties which include: anchorage-independent cell cycle progression, tumor cell invasion and apoptosis. ILK1 can also be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Furthermore, ILK1 phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
      ILK1 interacts with the cytoplasmic domains of integrin ?1 and ?3 subunits in addition to several adaptors and signaling proteins, it also acts as a proximal receptor kinase regulating integrin-mediated signal transduction. ILK1 is a focal adhesion protein part of the complex ILK-PINCH. This complex is deemed to be one of the convergence points of integrin- and growth factor-signaling pathway. ILK1 is stimulated rapidly but briefly by both cell fibronectin interactions in a PI3-K-dependent manner, probably through the binding of PtdIns(3,4,5)P3 with a PH-like domain of ILK.
      ILK1 over-expression has been documented in a wide variety of human malignancies.

    • Synonyms

      Integrin-linked protein kinase, ILK-1, ILK-2, 59 kDa serine/threonine-protein kinase, p59ILK, ILK, ILK1, ILK2, DKFZp686F1765, P59.

    • 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. Please avoid freeze thaw cycles.

    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.

    Ilk1 Human
  • View Data Sheet

    Name :

    Inhibin a Human

    Description:

    Inhibin Alpha Human Recombinant

    Product # :

    HOR-303

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    Description

    Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

    Purity

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

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      Alpha chain:
      STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

      Beta Chain:
      GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
      GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    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.

    Inhibin A Human
  • View Data Sheet

    Name :

    PI16 Human

    Description:

    Peptidase Inhibitor 16 Human Recombinant

    Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    Product # :

    ENZ-113

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    Description

    The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.

    • Synonyms

      Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PI16 Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.

    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.

    Pi16 Human
  • View Data Sheet

    Name :

    TIMP1 Human, Sf9

    Description:

    Tissue Inhibitor of Metalloprotease 1 Human Recombinant, Sf9

    TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 1.

    Product # :

    ENZ-876

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    Description

    TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (24-207a.a.) and having a molecular mass of 21.5kDa. TIMP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIMP1 protein solution (0.2mg/ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones.
      Increased TIMP1 levels are connected with squamous cell laryngeal carcinoma. TIMP1 overexpression is linked to gastric cancer.

    • Synonyms

      TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 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. Please avoid freeze thaw cycles.

    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.

    Timp1 Human Sf9
  • View Data Sheet

    Name :

    KRT18 Human, His

    Description:

    Cytokeratin 18 Human Recombinant , His Tag

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-484

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    Description

    KRT18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 52.42kDa.The KRT18 is fused to a His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT18 protein solution (0.8mg/ml) contains 20mM Tris pH 8, 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • 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. Please avoid freeze thaw cycles.

    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.

    Krt18 Human His
  • View Data Sheet

    Name :

    TPA (311-562) Human

    Description:

    Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

    Product # :

    ENZ-1023

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    Description

    TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 261 amino acids (311-562 a.a.) and having a molecular mass of 29.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).TPA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TPA protein solution (0.5mg/ml) contains 50mM MES (pH 5.0), 5mM CaCl2, 1mM DTT, 0.5M NaCl and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

    • 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

      ADPIKGGLFA DIASHPWQAA IFAKHRRSPG ERFLCGGILI SSCWILSAAH CFQERFPPHH LTVILGRTYR VVPGEEEQKF EVEKYIVHKE FDDDTYDNDI ALLQLKSDSS RCAQESSVVR TVCLPPADLQ LPDWTECELS GYGKHEALSP FYSERLKEAH VRLYPSSRCT SQHLLNRTVT DNMLCAGDTR SGGPQANLHD ACQGDSGGPL VCLNDGRMTL VGIISWGLGC GQKDVPGVYT KVTNYLDWIR DNMRPHHHHH H.

    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.

    Tpa 311 562 Human
  • View Data Sheet

    Name :

    CD79B Human, Sf9

    Description:

    CD79B Human Recombinant, Sf9

    CD79b Molecule, CD79B Antigen (Immunoglobulin-Associated Beta), CD79b Molecule, Immunoglobulin-Associated Beta, Immunoglobulin-Associated B29 Protein, B-Cell-Specific Glycoprotein B29, Ig-Beta, IGB, B29, B-Cell Antigen Receptor Complex-Associated Protein Beta Chain, CD79b Antigen, CD79B, AGM6.

    Product # :

    PRO-2404

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    Description

    CD79B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 140 amino acids (29-159a.a.) and having a molecular mass of 16.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).CD79B is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD79B protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD79B is a 36 kDa trans membrane glycoprotein belonging to the immunoglobulin superfamily. Heterodimers of CD79A and CD79B connect with a membrane attached immunoglobulin on the B cell surface to create the B cell antigen receptor complex (BCR). CD79A and CD79B are essential for BCR-mediated signaling and subsequently for the development and activation of B lineage cells.

    • Synonyms

      CD79b Molecule, CD79B Antigen (Immunoglobulin-Associated Beta), CD79b Molecule, Immunoglobulin-Associated Beta, Immunoglobulin-Associated B29 Protein, B-Cell-Specific Glycoprotein B29, Ig-Beta, IGB, B29, B-Cell Antigen Receptor Complex-Associated Protein Beta Chain, CD79b Antigen, CD79B, AGM6.

    • 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

      ADPARSEDRY RNPKGSACSR IWQSPRFIAR KRGFTVKMHC YMNSASGNVS WLWKQEMDEN PQQLKLEKGR MEESQNESLA TLTIQGIRFE DNGIYFCQQK CNNTSEVYQG CGTELRVMGF STLAQLKQRN TLKDHHHHHH.

    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.

    Cd79B Human Sf9
  • View Data Sheet

    Name :

    TREM2 Human

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-1794

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    Description

    TREM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (19-161 a.a) and having a molecular mass of 20.4kDa.TREM2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TREM2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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 KDRWGSHMHN TTVFQGVAGQ SLQVSCPYDS MKHWGRRKAW CRQLGEKGPC QRVVSTHNLW LLSFLRRWNG STAITDDTLG GTLTITLRNL QPHDAGLYQC QSLHGSEADT LRKVLVEVLA DPLDHRDAGD LWFPGESESF EDAHVEHSIS R.

    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.

    Trem2 Human
  • View Data Sheet

    Name :

    PRKCI Human

    Description:

    Protein Kinase C Iota Human Recombinant

    DXS1179E, nPKC-iota, PKCI, aPKC-lambda/iota, PRKC-lambda/iota, PRKCL, Protein kinase C iota type, Protein Kinase C iota, Atypical protein kinase C-lambda/iota, PRKCI.

    Product # :

    PKA-132

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PRKCI Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (1-596 a.a) containing a total of 602 amino acids, having a molecular mass of 69kDa. PRKCI is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRKCI, AKAPKC iota, is part of serine/threonine protein kinases family. It takes a key regulatory role in a number of cellular functions including hormone secretion,cell growth differentiation, and gene expression. It is involved in cell polarization processes and the formation of epithelial tight junctions.This protein kinase is calcium-independent and phospholipid-dependent. It is also implicated in the activation of several signal-pathways such as Ras, and NF-kappa-B, c-Src pathways.

    • Synonyms

      DXS1179E, nPKC-iota, PKCI, aPKC-lambda/iota, PRKC-lambda/iota, PRKCL, Protein kinase C iota type, Protein Kinase C iota, Atypical protein kinase C-lambda/iota, PRKCI.

    • 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

      MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPQEPV MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECVHHHH 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.

    Prkci Human
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