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Search results

1000 results found for “Parkinson Disease Protein”

Name

Description

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  • View Data Sheet

    Name :

    GDF6 Human

    Description:

    Bone Morphogenetic protein-13 Human Recombinant

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

    Product # :

    CYT-938

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    Shipped at Room temp

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

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

      Abstract:

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

      Introduction:

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

      Characteristics and Signaling Pathways:

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

      Production of BMP-13 Human Recombinant:

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

      Potential Therapeutic Applications:

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

      Conclusion:

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

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

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

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

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

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

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

      What is the endotoxin level for GDF6 Protein?

      The endotoxin level is minimal, GDF6 Protein was purified using conventional chromatography techniques.

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

    Bmp13 Human
  • View Data Sheet

    Name :

    GADD45GIP1 Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

    Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    Product # :

    PRO-972

    Price :

    Quantity :

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    Shipped with Ice Packs

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    • description
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    • More Info

    Description

    GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

    • Synonyms

      Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    • 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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

    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.

    Gadd45Gip1 Human
  • View Data Sheet

    Name :

    DNALI1 Human

    Description:

    Dynein Axonemal Light Intermediate Chain 1 Human Recombinant

    Dynein, Axonemal, Light Intermediate Chain 1, DJ423B22.5 (Axonemal Dynein Light Chain (Hp28)), Inner Dynein Arm Light Chain Axonemal, hp28, P28, Homolog Of Clamydomonas, Axonemal Dynein Light Intermediate Polypeptide 1, dJ423B22.5, Inner Dynein Arm, Homolog Of Clamydomonas, Dynein, Axonemal, Light Intermediate Polypeptide 1.

    Product # :

    PRO-1756

    Price :

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    Description

    DNALI1 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 34.2kDa. DNALI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DNALI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dynein Axonemal Light Intermediate Chain1 also known as DNALI1 belongs to the inner dynein arm light chain family. DNALI1 take a dynamic role in flagellar motility. DNALI1 is the human homolog of the Chlamydomonas inner dynein arm gene, p28. The exactfunction of DNALI1 is not known yet, on the other hand, it is a potential candidate for immotile cilia syndrome. In addition it has been found that the following diseases: primary ciliary dyskinesia, and huntington's disease have been associated with DNALI1. Ultrastructural defects of the inner dynein arms are seen in patients with ICS. Immotile mutant strains ofChlamydomonas, biflagellated algae, show similar defects.

    • Synonyms

      Dynein, Axonemal, Light Intermediate Chain 1, DJ423B22.5 (Axonemal Dynein Light Chain (Hp28)), Inner Dynein Arm Light Chain Axonemal, hp28, P28, Homolog Of Clamydomonas, Axonemal Dynein Light Intermediate Polypeptide 1, dJ423B22.5, Inner Dynein Arm, Homolog Of Clamydomonas, Dynein, Axonemal, Light Intermediate Polypeptide 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 MGSMVTANKA HTGQGSCWVA TLASAMIPPA DSLLKYDTPV LVSRNTEKRS PKARLLKVSP QQPGPSGSAP QPPKTKLPST PCVPDPTKQA EEILNAILPP REWVEDTQLW IQQVSSTPST RMDVVHLQEQ LDLKLQQRQA RETGICPVRR ELYSQCFDEL IREVTINCAE RGLLLLRVRD EIRMTIAAYQ TLYESSVAFG MRKALQAEQG KSDMERKIAE LETEKRDLER QVNEQKAKCE ATEKRESERR QVEEKKHNEE IQFLKRTNQQ LKAQLEGIIA PKK

    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.

    Dnali1 Human
  • View Data Sheet

    Name :

    KISS1 Human

    Description:

    KISS-1 Metastasis-Suppressor Human Recombinant

    Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.

    Product # :

    PRO-419

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    Description

    KISS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (20-138) and having a molecular mass of 12.6 Dalton. The KISS1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      KISS1 is a metastasis suppressor protein that suppresses metastases of melanomas and breast carcinomas without affecting tumorigenicity.KISS1 functions to inhibit chemotaxis and invasion, attenuating metastasis in malignant melanomas. KISS1 is involved in the regulation of cell-matrix adhesion. KISS1 plays a role in cytoskeletal reorganization. A polymorphism in the terminal exon of KISS1 mRNA results in two protein isoforms. Expression of KiSS1 is localized to specific regions of the hypothalamus in numerous species and is regulated by gonadal steroids and across the estrous cycle..KISS1 generates a c-terminally amidated peptide, metastin which functions as the endogenous ligand of the g-protein coupled receptor gpr54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis.

    • Synonyms

      Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MEPLEKVASV GNSRPTGQQL ESLGLLAPGE QSLPCTERKP AATARLSRRG TSLSPPPESS GSPQQPGLSA PHSRQIPAPQ GAVLVQREKD LPNYNWNSFG LRFGKREAAP GNHGRSAGRG.

    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.

    Kiss1 Human
  • View Data Sheet

    Name :

    TREM1 Human

    Description:

    Triggering Receptor Expressed on Myeloid Cells 1 Human Recombinant

    Triggering receptor expressed on myeloid cells 1, Triggering receptor expressed on monocytes 1, TREM-1, TREM1.

    Product # :

    PRO-457

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    Description

    TREM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (21-205 a.a.) and having a molecular mass of 23.3kDa.TREM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TREM1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
      TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.

    • Synonyms

      Triggering receptor expressed on myeloid cells 1, Triggering receptor expressed on monocytes 1, TREM-1, TREM1.

    • 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 MGSMATKLTE EKYELKEGQT LDVKCDYTLE KFASSQKAWQ IIRDGEMPKT LACTERPSKN SHPVQVGRII LEDYHDHGLL RVRMVNLQVE DSGLYQCVIY QPPKEPHMLF DRIRLVVTKG FSGTPGSNEN STQNVYKIPP TTTKALCPLY TSPRTVTQAP PKSTADVSTP DSEINLTNVT DIIRVPVFN.

    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.

    Trem1 Human
  • View Data Sheet

    Name :

    STX1A Human

    Description:

    Syntaxin-1A Human Recombinant

    STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    Product # :

    PRO-574

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    Description

    Syntaxin-1A Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-226) and having a molecular mass of 26.1 kDa.Recombinant Human STX1A contains N-terminal domain (Habc) and t_SNARE domain (H3 domain).

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 10% glycerol, and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

    • Synonyms

      STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    • 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

      MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ.

    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.

    Stx1A Human
  • View Data Sheet

    Name :

    SP100 Human

    Description:

    SP100 Recombinant Human

    Nuclear dot-associated Sp100 protein, SP100 nuclear antigen, Speckled 100 kDa, SP100-HMG nuclear autoantigen, FLJ00340, Lysp100b.

    Product # :

    PRO-108

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    Description

    Recombinant Sp100 antigen is a full-length cDNA coding having a molecular mass of 54,662 Dalton (pH 5.0).Shows a 79kDa band on SDS-PAGE. Sp100 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    Sp100 is supplied in 16mM HEPES buffer pH-8.0, 400mM NaCl, and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      SP100 protein is Homodimer which takes part in the control of gene expression. SP100 interacts with members of the HP1 family of nonhistone chromosomal protein, such as CBX5 and CBX3 via the PxVxL motif and also interacts with Epstein-Barr virus EBNA-LP.
      The major isoform Sp100-A, has a calculated MW of 54 kDa, but exhibits aberrant electrophoretic mobilities, with an apparent MW OF 100 kDa.

    • Synonyms

      Nuclear dot-associated Sp100 protein, SP100 nuclear antigen, Speckled 100 kDa, SP100-HMG nuclear autoantigen, FLJ00340, Lysp100b.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test.

    • coating concentration

      0.5-0.9 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with PBC sera or monoclonal anti-hexa-His-tag antibody.

    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.

    Sp100 Human
  • View Data Sheet

    Name :

    CRK Human

    Description:

    V-crk Sarcoma Virus CT10 Oncogene Human Recombinant

    Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

    Product # :

    PRO-275

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    Description

    CRK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids (1-204 a.a.) and having a molecular mass of 25kDa. The CRK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRK solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.

    • Synonyms

      Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL IGGR.

    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.

    CRK Human
  • View Data Sheet

    Name :

    SPARC Human

    Description:

    Secreted Protein Acidic & Rich in Cysteine Recombinant Human

    Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

    Product # :

    PRO-2602

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    Description

    Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC 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 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.

    More Info

    • Introduction

      SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

    • Synonyms

      Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.

    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.

    Sparc Protein
  • 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 :

    DCTN2 (1-406) Human

    Description:

    Dynactin 2 (1-406 a.a.) Human Recombinant

    DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.

    Product # :

    PRO-1820

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    Description

    Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (1-406 a.a) and having a molecular mass of 47.2kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

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

    • Synonyms

      DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAFA QELEELTSTS VEHIIVNPNA AYDKFKDKRV GTKGLDFSDR IGKTKRTGYE SGEYEMLGEG LGVKETPQQK YQRLLHEVQE LTTEVEKIKT TVKESATEEK LTPVLLAKQL AALKQQLVAS HLEKLLGPDA AINLTDPDGA LAKRLLLQLE ATKNSKGGSG GKTTGTPPDS SLVTYELHSR PEQDKFSQAA KVAELEKRLT ELETAVRCDQ DAQNPLSAGL QGACLMETVE LLQAKVSALD LAVLDQVEAR LQSVLGKVNE IAKHKASVED ADTQSKVHQL YETIQRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAN SLKDNTTLLT QVQTTMRENL ATVEGNFASI DERMKKLGK.

    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.

    Dctn2 1 406 Human
  • View Data Sheet

    Name :

    Prelamin-A

    Description:

    Prelamin-A Recombinant

    Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    Product # :

    PRO-689

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    Description

    Recombinant Prelamin-A is a 74kDa precursor of the nuclear lamin A protein. Prelamin-A is a structural component of the nuclear lamina and it is encoded by lamin A/C gene (LMNA). Due to the presence of a CAAX box sequence at carboxyl terminus, Prelamin-A in vivo goes through a serial of post-translational modifications, resulting in the farnesylation of the cysteine thiol, removal of the AAX tripeptide, carboxyl-methylation of the cysteinyl carboxy group and proteolysis of 18 C-terminal amino acids residues that lead to mature lamin A. Diverse mutations in the lamin A/C gene are associated with different deseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. Recombinant human prelamin A is fused to a 6 Histidine tag at the N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The Prelamin-A solution (0.1mg/ml) contains 10% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    • 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

      HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
      EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
      RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
      QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
      LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
      RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
      TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
      KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
      WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
      RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYL
      LGNSSPRTQSPQNCSIM

    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.

    Prelamin A
  • View Data Sheet

    Name :

    GOPC Human

    Description:

    Golgi-Associated PDZ and Coiled-Coil Motif Containing Human Recombinant

    CAL, dJ94G16.2, FIG, GOPC1, PIST, Golgi-associated PDZ and coiled-coil motif-containing protein, PDZ protein interacting specifically with TC10, CFTR-associated ligand, Fused in glioblastoma, GOPC.

    Product # :

    PRO-793

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    Description

    GOPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (278-454 a.a.) and having a molecular mass of 21.5 kDa. The GOPC is fused to a 20 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The GOPC protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GOPC is a PDZ domain-containing Golgi protein which binds the extreme C terminus of proteins in a sequence-specific manner. GOPC participates in intracellular protein trafficking and degradation. GOPC regulates CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. GOPC regulates the intracellular trafficking of the ADR1B receptor. GOPC takes part in autophagy. GOPC over expression results in CFTR intracellular retention and degradation in the lysosomes.

    • Synonyms

      CAL, dJ94G16.2, FIG, GOPC1, PIST, Golgi-associated PDZ and coiled-coil motif-containing protein, PDZ protein interacting specifically with TC10, CFTR-associated ligand, Fused in glioblastoma, GOPC.

    • 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 MIRKVLLLKE DHEGLGISIT GGKEHGVPIL ISEIHPGQPA DRCGGLHVGD AILAVNGVNL RDTKHKEAVT ILSQQRGEIE FEVVYVAPEV DSDDENVEYE DESGHRYRLY LDELEGGGNP GASCKDTSGE IKVLQGFNKK AVTDTHENGD LGTASETPLD DGASKLDDLH TLYHKKSY.

    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.

    Gopc Human
  • View Data Sheet

    Name :

    MINA Human

    Description:

    MYC Induced Nuclear Antigen Human Recombinant

    MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    Product # :

    PRO-2078

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    Description

    MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MINA protein solution (0.25mg/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

      MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.

    • Synonyms

      MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.

    • 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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.

    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.

    Mina Human
  • View Data Sheet

    Name :

    MAPRE3 Human

    Description:

    Microtubule-Associated Protein, RP/EB Family, Member 3 Human Recombinant

    RP3, EB3, EBF3, End-binding protein 3, EBF3-S, APC binding protein.

    Product # :

    PRO-264

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    Description

    MAPRE3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (1-281a.a.) and having a molecular mass of 34.1kDa.MAPRE3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPRE3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPRE3 is a microtubule related protein that cooperates with the colorectal adenomatous polyposis coli tumor suppressor protein and takes a curtail part in regulating microtubule dynamics, cell polarity, and chromosome stability. MAPRE3 protein is related to MAPRE1 and also associates with the microtubule cytoskeleton. MAPRE3 is expressed mainly in the central nervous system and specially associates with APCL, a homolog of the adenomatous polyposis coli tumor suppressor protein.

    • Synonyms

      RP3, EB3, EBF3, End-binding protein 3, EBF3-S, APC binding 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP PCILRKNPPS ARNGGHETDA QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y

    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.

    Mapre3 Human
  • View Data Sheet

    Name :

    PTPRN Human

    Description:

    Protein Tyrosine Phosphatase Receptor Type N Human Recombinant

    Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.

    Product # :

    ENZ-1162

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    Description

    Recombinant Human Protein Tyrosine Phosphatase Receptor Type N produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. PTPRN is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PTPRN is supplied in 50mM Sodium phosphate (pH 8.0) and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.

    • Synonyms

      Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.

    • 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. Avoid multiple 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.

    Ptprn Human
  • View Data Sheet

    Name :

    OmpA

    Description:

    Outer Membrane Protein-A Bacterial Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-571

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Outer Membrane Protein A
  • View Data Sheet

    Name :

    KPNA2 Human

    Description:

    Karyopherin Alpha 2 Human Recombinant

    Karyopherin subunit alpha 2 (RAG cohort 1 importin alpha 1), RCH1, QIP2, IPOA1, SRP1 alpha, RAG cohort protein 1, importin alpha 1, importin subunit alpha-2, importin-alpha-P1, pendulin.

    Product # :

    PRO-1032

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    Description

    KPNA2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 553 amino acids (1-529) and having a molecular mass of 60.5kDa.KPNA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The KPNA2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      KPNA2 belongs to the karyopherin alpha family. KPNA2 has a vital part in the nuclear import of proteins with a conventional nuclear localization signal (NLS).
      In vitro, KPNA2 bound specifically and directly to substrates having a simple or bipartite NLS motif. KPNA2 stimulated docking of import substrates to the nuclear envelope and together with Ran reconstituted complete nuclear protein import.

    • Synonyms

      Karyopherin subunit alpha 2 (RAG cohort 1 importin alpha 1), RCH1, QIP2, IPOA1, SRP1 alpha, RAG cohort protein 1, importin alpha 1, importin subunit alpha-2, importin-alpha-P1, pendulin.

    • 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 MGSHMSTNEN ANTPAARLHR FKNKGKDSTE MRRRRIEVNV ELRKAKKDDQ MLKRRNVSSF PDDATSPLQE NRNNQGTVNW SVDDIVKGIN SSNVENQLQA TQAARKLLSR EKQPPIDNII RAGLIPKFVS FLGRTDCSPI QFESAWALTN IASGTSEQTK VVVDGGAIPA FISLLASPHA HISEQAVWAL GNIAGDGSVF RDLVIKYGAV DPLLALLAVP DMSSLACGYL RNLTWTLSNL CRNKNPAPPI DAVEQILPTL VRLLHHDDPE VLADTCWAIS YLTDGPNERI GMVVKTGVVP QLVKLLGASE LPIVTPALRA IGNIVTGTDE QTQVVIDAGA LAVFPSLLTN PKTNIQKEAT WTMSNITAGR QDQIQQVVNH GLVPFLVSVL SKADFKTQKE AVWAVTNYTS GGTVEQIVYL VHCGIIEPLM NLLTAKDTKI ILVILDAISN IFQAAENLGE TEKLSIMIEE CGGLDKIEAL QNHENESVYK ASLSLIEKYF SVEEEEDQNV VPETTSEGYT FQVQDGAPGT FNF.

    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.

    Kpna2 Human
  • View Data Sheet

    Name :

    T.pallidum p41 Mosaic

    Description:

    Treponema pallidum p41 Mosaic Recombinant

    Product # :

    TRP-244

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    Description

    The E.coli derived recombinant protein contains the outer membrane T.Pallidum p41 immunodominant regions. The protein is fused with a GST tag.

    Source

    Escherichia Coli.

    Formulation

    25mM Tris-HCl pH-8, 60mM NaCl & 50% glycerol.

    Purity

    Treponema Pallidum protein is >90% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

      Treponema Pallidum protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T. Pallidum with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of T.Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum protein was purified by proprietary chromatographic technique.

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

    Tpallidum P41 Mosaic
  • View Data Sheet

    Name :

    ATF Human

    Description:

    Apo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    Product # :

    PRO-325

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    Description

    Human Apo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be <6 ppm.

    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.

    Apo Transferrin Human
  • View Data Sheet

    Name :

    MAVS Human

    Description:

    Mitochondrial Antiviral Signaling Protein Human Recombinant

    CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    Product # :

    PRO-1351

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    Description

    MAVS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 536 amino acids (1-513) and having a molecular mass of 55.9 kDa. MAVS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial antiviral signaling protein (MAVS) is vital for innate immune defense against viruses. MAVS is an intermediary protein essential in the virus-triggered IFN-beta signaling pathways. MAVS is involved in activation of transcription factors that regulate expression of IFN-beta and contributes to antiviral immunity.

    • Synonyms

      CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    • 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 MGSMPFAEDK TYKYICRNFS NFCNVDVVEI LPYLPCLTAR DQDRLRATCT LSGNRDTLWH LFNTLQRRPG WVEYFIAALR GCELVDLADE VASVYQSYQP RTSDRPPDPL EPPSLPAERP GPPTPAAAHS IPYNSCREKE PSYPMPVQET QAPESPGENS EQALQTLSPR AIPRNPDGGP LESSSDLAAL SPLTSSGHQE QDTELGSTHT AGATSSLTPS RGPVSPSVSF QPLARSTPRA SRLPGPTGSV VSTGTSFSSS SPGLASAGAA EGKQGAESDQ AEPIICSSGA EAPANSLPSK VPTTLMPVNT VALKVPANPA SVSTVPSKLP TSSKPPGAVP SNALTNPAPS KLPINSTRAG MVPSKVPTSM VLTKVSASTV PTDGSSRNEE TPAAPTPAGA TGGSSAWLDS SSENRGLGSE LSKPGVLASQ VDSPFSGCFE DLAISASTSL GMGPCHGPEE NEYKSEGTFG IHVAENPSIQ LLEGNPGPPA DPDGGPRPQA DRKFQEREVP CHRPSP.

    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.

    Mavs Human
  • View Data Sheet

    Name :

    PICK1 Human

    Description:

    Protein Interacting With PRKCA 1 Human Recombinant

    Protein Interacting With PRKCA 1, PRKCABP, Protein Kinase C-Alpha-Binding Protein, Protein Interacting With C Kinase 1, Protein Kinase C, Alpha Binding Protein, Protein Interacting With PRKCA, PRKCA-Binding Protein, PICK, PRKCA-binding protein.

    Product # :

    PKA-072

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    Description

    PICK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 438 amino acids (1-415 a.a) and having a molecular mass of 49.0kDa. PICK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PICK1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Interacting with PRKCA 1, also known as PICK1 includes a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). PICK1 performs as an adaptor which binds to and arranges the subcellular localization of various membrane proteins. PICK1 interacts with multiple glutamate receptor subtypes, monoamine plasma membrane transporters, in addition to non-voltage gated sodium channels, and might target PRKCA to these membrane proteins and therefore regulates their distribution as well as function. PICK1 has also been found to perform as an anchoring protein which particularly targets PRKCA to mitochondria in a ligand-specific manner.

    • Synonyms

      Protein Interacting With PRKCA 1, PRKCABP, Protein Kinase C-Alpha-Binding Protein, Protein Interacting With C Kinase 1, Protein Kinase C, Alpha Binding Protein, Protein Interacting With PRKCA, PRKCA-Binding Protein, PICK, PRKCA-binding 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 MGSMFADLDY DIEEDKLGIP TVPGKVTLQK DAQNLIGISI GGGAQYCPCL YIVQVFDNTP AALDGTVAAG DEITGVNGRS IKGKTKVEVA KMIQEVKGEV TIHYNKLQAD PKQGMSLDIV LKKVKHRLVE NMSSGTADAL GLSRAILCND GLVKRLEELE RTAELYKGMT EHTKNLLRAF YELSQTHRAF GDVFSVIGVR EPQPAASEAF VKFADAHRSI EKFGIRLLKT IKPMLTDLNT YLNKAIPDTR LTIKKYLDVK FEYLSYCLKV KEMDDEEYSC IALGEPLYRV STGNYEYRLI LRCRQEARAR FSQMRKDVLE KMELLDQKHV QDIVFQLQRL VSTMSKYYND CYAVLRDADV FPIEVDLAHT TLAYGLNQEE FTDGEEEEEE EDTAAGEPSR DTRGAAGPLD KGGSWCDS.

    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.

    Pick1 Human
  • View Data Sheet

    Name :

    TRIB3 Human

    Description:

    Tribbles Pseudokinase 3 Human Recombinant

    Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Tribbles homolog 3.

    Product # :

    PKA-070

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    Description

    TRIB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 42.0kDa. TRIB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TRIB3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Tribbles Pseudokinase 3, also known as TRIB3, is a putative protein kinase which is induced by the transcription factor NF-kappaB. In addition, TRIB3 is a negative regulator of NF-kappaB, and can as well sensitize cells to TNF- and TRAIL-induced apoptosis. Furthermore, TRIB3 is able to negatively regulate the cell survival serine-threonine kinase AKT1. One of the diseases which are associated with TRIB3 is anoxia.

    • Synonyms

      Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Tribbles homolog 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 MGSMRATPLA APAGSLSRKK RLELDDNLDT ERPVQKRARS GPQPRLPPCL LPLSPPTAPD RATAVATASR LGPYVLLEPE EGGRAYQALH CPTGTEYTCK VYPVQEALAV LEPYARLPPH KHVARPTEVL AGTQLLYAFF TRTHGDMHSL VRSRHRIPEP EAAVLFRQMA TALAHCHQHG LVLRDLKLCR FVFADRERKK LVLENLEDSC VLTGPDDSLW DKHACPAYVG PEILSSRASY SGKAADVWSL GVALFTMLAG HYPFQDSEPV LLFGKIRRGA YALPAGLSAP ARCLVRCLLR REPAERLTAT GILLHPWLRQ DPMPLAPTRS HLWEAAQVVP DGLGLDEARE EEGDREVVLY G.

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

    Trib3 Human
  • View Data Sheet

    Name :

    CALM Human

    Description:

    Calmodulin Human

    Calmodulin, CaM, CALM.

    Product # :

    PRO-2799

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    Source

    Human brain tissue.

    Formulation

    CALM was lyophilized with 2mM EDTA.

    Purity

    Greater than 95.0%.

    More Info

    • Synonyms

      Calmodulin, CaM, CALM.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

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

    • Background

      Calmodulin, a small, ubiquitous calcium-binding protein, stands as a linchpin in cellular signalling cascades. Its ability to modulate diverse cellular processes by transducing calcium signals has made it a focal point of scientific inquiry. With its role extending from muscle contraction to neurotransmitter release and gene expression, calmodulin orchestrates intricate physiological responses. This research delves into the multifaceted world of calmodulin, exploring its structural characteristics, calcium-binding properties, and its pivotal involvement in various biological pathways.

      Structural Marvel of Calmodulin:

      Calmodulin boasts a unique dumbbell-shaped structure, composed of four EF-hand motifs that enable it to bind calcium ions. When calcium binds to calmodulin, it undergoes a conformational change, allowing it to interact with a myriad of target proteins. This structural adaptability is fundamental to its ability to regulate a wide array of cellular activities.

      Calcium Signalling and Transduction:

      Intracellular calcium serves as a ubiquitous second messenger, and calmodulin is the key mediator of calcium signalling. When calcium levels rise, calmodulin binds calcium ions, triggering its activation. This activated form of calmodulin modulates the activity of various proteins, including enzymes, ion channels, and transcription factors. By doing so, calmodulin influences processes such as muscle contraction, neurotransmitter release, and cell proliferation.

    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.

    Calmodulin Human
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