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1000 results found for “calmodulin”
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Name :
Activin-A RatDescription:
Activin-A Rat Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-147Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/mlMore Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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.
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Name :
GADD45GIP1 HumanDescription:
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-972Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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
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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.
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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.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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Name :
Super Leptin qA OvineDescription:
Super Leptin Antagonist Ovine Recombinant
Product # :
CYT-1245Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Ovine leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Ovine leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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.
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Name :
TECK Human, HisDescription:
Thymus Expressed Chemokine (CCL25) Human Recombinant, His Tag
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-032Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (24-150 a.a.) and having a molecular mass of 16.8kDa.TECK is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TECK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.
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.
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Name :
CCDC25 HumanDescription:
Coiled-Coil Domain Containing 25 Human Recombinant
Coiled-coil domain-containing protein 25, CCDC25.
Product # :
PRO-1655Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.
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Synonyms
Coiled-coil domain-containing protein 25, CCDC25.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.
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.
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Name :
ACTN1 HumanDescription:
Actinin Alpha 1 Human Recombinant
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.
Product # :
PRO-2227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.
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Synonyms
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.
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.
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Name :
SLAMF1 HumanDescription:
SLAMF1 Human Recombinant
Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.
Product # :
PRO-1342Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SLAMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (21-237 a.a) and having a molecular mass of 26.7kDa.SLAMF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SLAMF1 protein solution (0.5mg/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
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Introduction
SLAMF1 is a member of the immunoglobulin gene superfamily and is involved in T-cell stimulation. The SLAMF1 protein is constitutively expressed on peripheral blood memory T cells, T-cell clones, immature thymocytes, and a fraction of B cells, and is swiftly induced on naive T cells after activation. There are probably 2 modes of SLAM signaling: one in which the inhibitor SH2D1A serves as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction functions.
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Synonyms
Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSASYGTGG RMMNCPKILR QLGSKVLLPL TYERINKSMN KSIHIVVTMA KSLENSVENK IVSLDPSEAG PPRYLGDRYK FYLENLTLGI RESRKEDEGW YLMTLEKNVS VQRFCLQLRL YEQVSTPEIK VLNKTQENGT CTLILGCTVE KGDHVAYSWS EKAGTHPLNP ANSSHLLSLT LGPQHADNIY ICTVSNPISN NSQTFSPWPG CRTDPSETKP.
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.
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Name :
FBLIM1 HumanDescription:
Filamin Binding LIM Protein 1 Human Recombinant
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
Product # :
PRO-1473Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FBLIM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373) and having a molecular mass of 43.1 kDa. FBLIM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FBLIM1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Filamin binding LIM protein 1 (FBLIM1) plays a role as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. FBLIM1 is involved in cell shape spreading and motility. FBLIM1 participates in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. FBLIM1 promotes stimulation of integrins and regulates integrin-mediated cell-cell adhesion.
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Synonyms
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASKPEK RVASSVFITL APPRRDVAVA EEVRQAVCEA RRGRPWEAPA PMKTPEAGLA GRPSPWTTPG RAAATVPAAP MQLFNGGCPP PPPVLDGEDV LPDLDLLPPP PPPPPVLLPS EEEAPAPMGA SLIADLEQLH LSPPPPPPQA PAEGPSVQPG PLRPMEEELP PPPAEPVEKG ASTDICAFCH KTVSPRELAV EAMKRQYHAQ CFTCRTCRRQ LAGQSFYQKD GRPLCEPCYQ DTLERCGKCG EVVRDHIIRA LGQAFHPSCF TCVTCARCIG DESFALGSQN EVYCLDDFYR KFAPVCSICE NPIIPRDGKD AFKIECMGRN FHENCYRCED CRILLSVEPT DQGCYPLNNH LFCKPCHVKR SAAGCC.
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.
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Name :
GDNF HumanDescription:
Glial-Derived Neurotrophic Factor Human Recombinant
ATF1, ATF2, HFB1-GDNF, GDNF.
Product # :
CYT-305Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- sds-page
Description
Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.
sds-page
More Info
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Introduction
GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake. -
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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.
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Solubility
It is recommended to reconstitute the lyophilized Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
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Background
What is the molecular weight/Mw of GDNF HUMAN Protein?
GDNF HUMAN Protein has a total Mw of 30kDa.
What is the source or expression system of GDNF HUMAN Protein?
Escherichia Coli.
What is the Purity of GDNF HUMAN Protein?
GDNF HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF HUMAN Protein?
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.
What is the amino acid sequence of GDNF HUMAN Protein?
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
What applications can GDNF HUMAN Protein be used in?
GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF HUMAN Protein?
The endotoxin level is minimal, GDNF HUMAN 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.
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Name :
PALM HumanDescription:
Paralemmin Human Recombinant
Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.
Product # :
PRO-2053Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PALM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (1-387) and having a molecular mass of 44.5kDa.PALM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PALM solution (0.5mg/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
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Introduction
Paralemmin (PALM) belongs to the paralemmin protein family which takes part in plasma membrane dynamics and cell process formation. The product of PALM is related with the cytoplasmic face of plasma membranes and is implicated in plasma membrane dynamics in neurons and other cell types.
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Synonyms
Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEVLAAE TTSQQERLQA IAEKRKRQAE IENKRRQLED ERRQLQHLKS KALRERWLLE GTPSSASEGD EDLRRQMQDD EQKTRLLEDS VSRLEKEIEV LERGDSAPAT AKENAAAPSP VRAPAPSPAK EERKTEVVMN SQQTPVGTPK DKRVSNTPLR TVDGSPMMKA AMYSVEITVE KDKVTGETRV LSSTTLLPRQ PLPLGIKVYE DETKVVHAVD GTAENGIHPL SSSEVDELIH KADEVTLSEA GSTAGAAETR GAVEGAARTT PSRREITGVQ AQPGEATSGP PGIQPGQEPP VTMIFMGYQN VEDEAETKKV LGLQDTITAE LVVIEDAAEP KEPAPPNGSA AEPPTEAASR EENQAGPEAT TSDPQDLDMK KHRCKCCSIM.
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.
- View Data Sheet
Name :
STC 1 HumanDescription:
Stanniocalcin-1 Human Recombinant
Stanniocalcin-1, STC, STC-1.
Product # :
HOR-259Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stanniocalcin-1 Human Recombinant produced in 293 cell line is a single, glycosylated, polypeptide chain containing 240 amino acids and having a total molecular mass of 25.9 kDa. The Stanniocalcin contains 10 residues form the C-Terminal Flag- tag. Stanniocalcin is purified by proprietary chromatographic techniques.
Source
293 cell line (Human embryonic kidney).
Formulation
Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Stanniocalcin 1 (STC1) is the mammalian homologue of STC, which was originally identified as a calcium/phosphate-regulating hormone in bony fishes. In contrast, STC1 may play an autocrine and paracrine role with pleiotropic effects in mammals. It is expressed in a wide variety of tissues, but unexpectedly is not detected in the circulation under normal circumstances, which is possibly caused by its attaching to soluble and tethered forms of a high-affinity binding protein. STC-1 can affect calcium homeostasis, bone and muscle mass and structure, and angiogenesis through effects on osteoblasts, osteoclasts, myoblasts/myocytes, and endothelial cells in mouse model. Differential regulation of myocardial STC1 protein expression was reported in heart failure. In addition, STC1 may regulate calcium currents in cardiomyocytes and may contribute to the alterations in calcium homeostasis of the failing heart. STC1 was found to be a selective modulator of hepatocyte growth factor (HGF)-induced endothelial migration and morphogenesis, an inhibitor of macrophage chemotaxis and chemokinesis, suppressor of progesterone and luteinization inhibitor. Together with STC-2, it may play important roles in the processes of implantation and decidualization in the rat. In terminally differentiated adipocytes, it may function as a "survival factor", which contributes to the maintenance of the integrity of mature adipose tissue. In context with its possible role in gestation, a Big STC, a three highermolecular- mass variant has been described. STC1 was identified as one of hypoxia-responsive genes coupled to hypoxia-driven angiogenesis.
Current research indicates that STC-1 might be a useful molecular marker to detect tumor cells in blood and bone marrow from patients with various types of malignancies. -
Synonyms
Stanniocalcin-1, STC, STC-1.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized STC-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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.
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Solubility
Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
THEAEQNDSV SPRKSRVAAQ NSAEVVRCLN SALQVGCGAF ACLENSTCDT DGMYDICKSF LYSAAKFDTQ GKAFVKESLK CIANGVTSKV FLAIRRCSTF QRMIAEVQEE CYSKLNVCSI AKRNPEAITE VVQLPNHFSN RYYNRLVRSL LECDEDTVST IRDSLMEKIG PNMASLFHIL QTDHCAQTHP RADFNRRRTN EPQKLKVLLR NLRGEEDSPS HIKRTSHESA ASDYKDDDDK.
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.
- View Data Sheet
Name :
MALD1Description:
Major Allergen Mal d 1 Recombinant (Mal d 1.0108)
Major allergen Mal d 1, Ypr10 protein, MALD1, ypr10, Mal d 1.0108
Product # :
ALR-013Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant MALD1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,492 Dalton. MALD1 purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MALD1 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
MALD1 is a ribonuclease and a heat-sensitive allergen which is a member of the pathogenesis-related protein class. MALD1 shares homologous IgE epitopes with major birch pollen allergen Bet v 1 and Cor a 1 from hazelnut pollen.
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Synonyms
Major allergen Mal d 1, Ypr10 protein, MALD1, ypr10, Mal d 1.0108
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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.
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Name :
MALD3Description:
Non-Specific Lipid-Transfer Protein Mal d 3 Recombinant
Non-specific lipid-transfer protein, LTP, MALD3.
Product # :
ALR-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Non-Specific Lipid-Transfer Protein Mal d 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 12kDa.MALD3 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MALD3 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
MALD3 (a non-specific lipid transfer protein) is a major apple allergen. LTPs are found mainly in aerial plant organs such as leaves, seeds, flowers, and fruit. MALD3 is a heat-stable protein which is characterized by having resistance to pepsin hydrolysis.
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Synonyms
Non-specific lipid-transfer protein, LTP, MALD3.
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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.
-
Immunological Functions
1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples
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Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
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.
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Name :
Activin A Human PlantDescription:
Activin A Human Recombinant, Plant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-052Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin A should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Activin A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.
What is the source or expression system of Activin A Protein?
Nicotinia
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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Serological Identification
The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.
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.
- View Data Sheet
Name :
NECTIN1 HumanDescription:
Nectin Cell Adhesion Molecule 1 Human Recombinant
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
Product # :
PRO-2648Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.
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Synonyms
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
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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.
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Amino Acid Sequence
ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VCAM1 MouseDescription:
Vascular cell adhesion molecule 1 Mouse Recombinant
V-CAM 1, VCAM-1, CD106, Vcam1, Vcam-1, Vascular cell adhesion protein 1.
Product # :
PRO-2257Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VCAM1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 682 amino acids (25-698 a.a) and having a molecular mass of 75.4kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). VCAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
VCAM1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).
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Synonyms
V-CAM 1, VCAM-1, CD106, Vcam1, Vcam-1, Vascular cell adhesion protein 1.
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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.
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Amino Acid Sequence
FKIEISPEYK TIAQIGDSMA LTCSTTGCES PLFSWRTQID SPLNAKVRTE GSKSVLTMEP VSFENEHSYL CTATCGSGKL ERSIHVDIYS FPKDPEIQFS GPLEVGKPVT VKCLAPDIYP VYRLEIDLFK GDQLMNRQEF SSEEMTKSLE TKSLEVTFTP VIEDIGKALV CRAKLHIDQI DSTLKERETV KELQVYISPR NTTISVHPST RLQEGGAVTM TCSSEGLPAP EIFWGRKLDN EVLQLLSGNA TLTLIAMRME DSGVYVCEGV NLIGRDKAEV ELVVQEKPFI VDISPGSQVA AQVGDSVVLT CAAIGCDSPS FSWRTQTDSP LNGVVRNEGA KSTLVLSSVG FEDEHSYLCA VTCLQRTLEK RTQVEVYSFP EDPVIKMSGP LVHGRPVTVN CTVPNVYPFD HLEIELLKGE TTLMKKYFLE EMGIKSLETK ILETTFIPTI EDTGKSLVCL ARLHSGEMES EPKQRQSVQP LYVNVAPKET TIWVSPSPIL EEGSPVNLTC SSDGIPAPKI LWSRQLNNGE LQPLSENTTL TFMSTKRDDS GIYVCEGINE AGISRKSVEL IIQVSPKDIQ LTVFPSKSVK EGDTVIISCT CGNVPETWII LKKKAKTGDM VLKSVDGSYT IRQAQLQDAG IYECESKTEV GSQLRSLTLD VKGKEHNKNY FSPELEHHHH 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.
- View Data Sheet
Name :
SMAC/DIABLO HumanDescription:
SMAC/DIABLO Human Recombinant
Diablo homolog mitochondrial, Second mitochondria-derived activator of caspase, Smac protein, Direct IAP-binding protein with low pI, DIABLO, SMAC, SMAC3, DIABLO-S, FLJ10537, FLJ25049.
Product # :
PRO-614Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Smac/Diablo Human Recombinant fused to N-terminal T7-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22 kDa.
Source
Escherichia Coli.
Formulation
The Smac/Diablo solution contains 20mM Tris pH-7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Smac/Diablo is a proapoptotic protein that increases caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway by its binding to the inhibitor of apoptosis proteins (IAPs) and removing their inhibitory activity. Smac/Diablo is a mitochondrial protein which enters the cytosol when cells go through apoptosis, and it moderates the caspase inhibition of IAPs.
Smac/DIABLO expression is associated with the result of renal cell carcinoma.
Dimeric form of Smac/DIABLO implies that once expressed in the cell the protein has a little probability of dissociation and, thus, loss of function.
Survivin, Smac/DIABLO, & PKC-? play an important part in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells. Mitochondrial survivin associates with Smac/DIABLO, delaying its release. Decreased expression of Smac protein takes part in ovarian carcinogenesis and chemotherapeutic resistance. Smac/DIABLO plays a role in tumor cells during the pathway of apoptosis induction. SMAC protein is regulated by XIAP and degraded by proteasome. SMAC protein takes part inleukemic cell apoptosis.
Smac is released during stress-induced apoptosis in multiple myeloma cells. -
Synonyms
Diablo homolog mitochondrial, Second mitochondria-derived activator of caspase, Smac protein, Direct IAP-binding protein with low pI, DIABLO, SMAC, SMAC3, DIABLO-S, FLJ10537, FLJ25049.
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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.
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Amino Acid Sequence
MASMTGGQQM GRGSMAVPIA QKSEPHSLSS EALMRRAVSL VTDSTSTFLS QTTYALIEAI TEYTKAVYTL TSLYRQYTSL LGKMNSEEED EVWQVIIGAR AEMTSKHQEY LKLETTWMTA VGLSEMAAEA AYQTGADQAS ITARNHIQLV KLQVEEVHQL SRKAETKLAE AQIEELRQKT QEEGEERAES EQEAYLRED.
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.
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Name :
S100A4 MouseDescription:
S100 Calcium Binding Protein A4 Mouse Recombinant
Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.
Product # :
PRO-229Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101 a.a) and having a molecular mass of 13.9kDa.S100A4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A4 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A4 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 belongs to the family of calcium binding proteins such as calmodulin and troponin C. S100A is composed of an alpha and beta chain whereas S100B is composed of two beta chains. S100 protein is also expressed in the antigen presenting cells such as the Langerhans cells in skin and interdigitating reticulum cells in the paracortex of lymph nodes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A4 may function in motility, invasion, and tubulin polymerization. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.
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Synonyms
Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MARPLEEALD VIVSTFHKYS GKEGDKFKLN KTELKELLTR ELPSFLGKRT DEAAFQKVMS NLDSNRDNEV DFQEYCVFLS CIAMMCNEFF EGCPDKEPRK K.
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.
- View Data Sheet
Name :
S100b HumanDescription:
S100 Calcium Binding Protein B Human Recombinant
S100 Calcium Binding Protein B, S-100 Protein Subunit Beta, S100 Calcium Binding Protein, Beta (Neural), S100 Calcium-Binding Protein, Beta (Neural), S-100 Calcium-Binding Protein, Beta Chain, S100 Calcium-Binding Protein B, S-100 Protein Beta Chain, S100beta, S100-B, S100, NEF.
Product # :
PRO-2312Price :
Quantity :
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Description
S100b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids (1-92 a.a.) and having a molecular mass of 10.7kDa. The S100b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100b protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.
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Synonyms
S100 Calcium Binding Protein B, S-100 Protein Subunit Beta, S100 Calcium Binding Protein, Beta (Neural), S100 Calcium-Binding Protein, Beta (Neural), S-100 Calcium-Binding Protein, Beta Chain, S100 Calcium-Binding Protein B, S-100 Protein Beta Chain, S100beta, S100-B, S100, NEF.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE.
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.
- View Data Sheet
Name :
CXCL16 HumanDescription:
CXCL16 Human Recombinant
Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.
Product # :
CHM-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL16 Human Recombinant (30-118 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids and having a molecular mass of 10kDa.The CXCL16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL16 protein was lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.More Info
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Introduction
CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.
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Synonyms
Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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.
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Solubility
It is recommended to reconstitute the lyophilized CXCL16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.
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Background
What is the molecular weight/Mw of CXCL16 HUMAN Protein?
CXCL16 HUMAN Protein has a total Mw of 10kDa.
What is the source or expression system of CXCL16 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL16 HUMAN Protein?
CXCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL16 HUMAN Protein?
The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.
What is the amino acid sequence of CXCL16 HUMAN Protein?
NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.
What applications can CXCL16 HUMAN Protein be used in?
CXCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL16 HUMAN Protein?
The endotoxin level is minimal, CXCL16 HUMAN 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.
- View Data Sheet
Name :
TAC3 HumanDescription:
Tachykinin-3 Human Recombinant
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
Product # :
PRO-716Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy. -
Synonyms
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.
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.
- View Data Sheet
Name :
NEFMDescription:
Neurofilament Medium Polypeptide Bovine
Neurofilament medium polypeptide, NF-M, Neurofilament triplet M protein, 160 kDa neurofilament protein, Neurofilament 3, NEFM, NEF3, NFM.
Product # :
PRO-523Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- purity
- More Info
Description
Ultra Pure NeuroFilament Protein having a Molecular mass of 160 kDa produced from Bovine Spinal Cord.
Source
Bovine Spinal Cord.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate, pH-7.5, 2mM DTT, 6M urea, 10mM methylammonium chloride and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Neurofilaments are type IV intermediate filament heteropolymers that are composed of light, medium, and heavy chains. Neurofilaments comprise the axoskeleton and functionally maintain neuronal caliber and may also have a role in intracellular transport to axons and dendrites.
NeuroFilament 160kDa is a medium neurofilament protein, which is commonly used as a biomarker of neuronal damage. -
Synonyms
Neurofilament medium polypeptide, NF-M, Neurofilament triplet M protein, 160 kDa neurofilament protein, Neurofilament 3, NEFM, NEF3, NFM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized NEFM between 2-8°C, do not freeze. Upon reconstitution NEFM should be stored below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NEFM in sterile 18MΩ-cm H2O.
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.
- View Data Sheet
Name :
Betacellulin His HumanDescription:
Betacellulin Human Recombinant, His Tag
Betacellulin, Probetacellulin.
Product # :
CYT-077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Synonyms
Betacellulin, Probetacellulin.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 11.3kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The biological functionality of BETACELLULIN Protein will be determined in the future.
What is the amino acid sequence of BETACELLULIN Protein?
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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.
- View Data Sheet
Name :
Thymosin a1 humanDescription:
Thymosin a1 Acetate
Product # :
HOR-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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.
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Solubility
It is recommended to reconstitute the lyophilized Thymosin a1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.
What is the Purity of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.
What applications can THYMOSIN-A1 HUMAN Protein be used in?
THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
The endotoxin level is minimal, THYMOSIN-A1 HUMAN 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.