Search results
1000 results found for “neuregulin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
SCRN1 HumanDescription:
Secernin 1 Human Recombinant
Secernin-1, SES1, KIAA0193, Secernin 1.
Product # :
PRO-2212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SCRN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 48.8kDa. SCRN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SCRN1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) , 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.
-
Synonyms
Secernin-1, SES1, KIAA0193, Secernin 1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
GSSHHHHHH SSGLVPRGSH MGSMAAAPPS YCFVAFPPRA KDGLVVFGKN SARPRDEVQE VVYFSAADHE PESKVECTYI SIDQVPRTYA IMISRPAWLW GAEMGANEHG VCIANEAINT REPAAEIEAL LGMDLVRLGL ERGETAKEAL DVIVSLLEEH GQGGNYFEDA NSCHSFQSAY LIVDRDEAWV LETIGKYWAA EKVTEGVRCI CSQLSLTTKM DAEHPELRSY AQSQGWWTGE GEFNFSEVFS PVEDHLDCGA GKDSLEKQEE SITVQTMMNT LRDKASGVCI DSEFFLTTAS GVSVLPQNRS SPCIHYFTGT PDPSRSIFKP FIFVDDVKLV PKTQSPCFGD DDPAKKEPRF QEKPDRRHEL YKAHEWARAI IESDQEQGRK LRSTMLELEK QGLEAMEEIL TSSEPLDPAE VGDLFYDCVD TEIKFFK.
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 :
NME3 Human, ActiveDescription:
Non-Metastatic Cells 3 Human Recombinant, BioActive
Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.
Product # :
PRO-2641Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
NME3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-169 a.a.) and having a molecular mass of 19.1kDa.NME3 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NME3 solution (0.5mg/ml) contains 50% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.
More Info
-
Introduction
Non-Metastatic Cells 3 or NME3 is a possible suppressor of metastasis. NME3 can be found at a lower levels in greatly metastatic cells when compared to cells that has less metastatic potential NME3 is crucial for the nucleoside triphosphates synthesis, also, in apoptosis induction & hematopoiesis. NME3 is can be expressed during early stages of myeloid differentiation of greatly purified CD34+ cells.
-
Synonyms
Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.
-
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 MERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA SEELLREHYA ELRERPFYGR LVKYMASGPV VAMVWQGLDV VRTSRALIGA TNPADAPPGT IRGDFCIEVG KNLIHGSDSV ESARREIALW FRADELLCWE DSAGHWLYE
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 :
SNRPG HumanDescription:
Small Nuclear Ribonucleoprotein Polypeptide G Human Recombinant
Small nuclear ribonucleoprotein G, snRNP-G, Sm protein G, Sm-G, SmG, SNRPG, PBSCG, MGC117317.
Product # :
PRO-196Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNRPG 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 96 amino acids (1-76 a.a.) and having a molecular mass of 10.6kDa. The SNRPG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNRPG solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Small nuclear ribonucleoprotein polypeptide G (SNRPG) is a member of the snRNP Sm proteins family. There are at least 7 isoforms, B/B, E, F, G, D1, D2, and D3. This class of common proteins has a vital role in the biogenesis of the snRNPs. The human Sm G genes are mapped to chromosomes 2. Furthermore, these proteins represent the major targets for the supposed anti-Sm auto-antibodies which are diagnostic for SLE (systemic lupus erythematosus). One class of these autoantibodies reacts specifically with native Sm E-F-G complexes.
-
Synonyms
Small nuclear ribonucleoprotein G, snRNP-G, Sm protein G, Sm-G, SmG, SNRPG, PBSCG, MGC117317.
-
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 MSKAHPPELK KFMDKKLSLK LNGGRHVQGI LRGFDPFMNL VIDECVEMAT SGQQNNIGMV VIRGNSIIML EALERV.
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 :
OrnipressinDescription:
Ornipressin
Product # :
HOR-036Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Ornipressin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1042.19 Dalton and a Molecular formula of C45H63N13O12 S2.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Ornipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Ornipressin 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 Ornipressin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
H-Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Orn-Gly-NH2.
-
Background
Ornipressin, a naturally occurring non-mammalian vasopressin analogue, has been recognized for its role in vasoconstriction and antidiuresis, making it an invaluable agent in certain clinical settings (Holmes et al., 2003). This paper aims to comprehensively review ornipressin's biochemical properties, its clinical applications, and potential future directions for therapeutic use.
Ornipressin is characterized by its strong vasopressin V1 receptor agonist activity, resulting in intense vasoconstriction. It also exhibits antidiuretic properties through the activation of V2 receptors in the renal collecting ducts, albeit to a lesser extent compared to vasopressin (Evans & Davidson, 1964).
Clinical applications of ornipressin are mainly driven by its potent vasoconstrictor activity. It has shown promise in managing esophageal variceal bleeding, where its vasoconstrictive properties help achieve hemostasis (Bosch et al., 2004).
Furthermore, it has been used as a rescue therapy in vasodilatory shock, where traditional vasoconstrictors may have limited effect (Morelli et al., 2005).
As our understanding of ornipressin continues to expand, future research is directed toward fine-tuning its application in various clinical scenarios and exploring potential new therapeutic roles. Current research is investigating the possible neuroprotective role of ornipressin in conditions such as cerebral ischemia (Uchida et al., 2010).Ornipressin, with its robust vasoconstrictor and antidiuretic properties, plays a crucial role in managing certain clinical situations. As we continue to explore this intriguing compound, its therapeutic potential appears to be far-reaching, warranting continued research in this field
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 :
NTRK2 Human , HEKDescription:
Neurotrophic Receptor Tyrosine Kinase 2, HEK Human Recombinant
GP145-TrkB, trk-B, TRKB, NTRK2.
Product # :
CYT-1230Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NTRK2 Human Recombinant is a single, glycosylated, polypeptide chain (32-430 a.a) containing a total of 632 amino acids and having a molecular mass of 70.3 kDa. NTRK2 is fused to a 233 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The NTRK2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Synonyms
GP145-TrkB, trk-B, TRKB, NTRK2.
-
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
CPTSCKCSAS RIWCSDPSPG IVAFPRLEPN SVDPENITEI FIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAHKAF LKNSNLQHIN FTRNKLTSLS RKHFRHLDLS ELILVGNPFT CSCDIMWIKT LQEAKSSPDT QDLYCLNESS KNIPLANLQI PNCGLPSANL AAPNLTVEEG KSITLSCSVA GDPVPNMYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVKGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL IAKNEYGKDE KQISAHFMGW PGIDDGANPN YPDVIYEDYG TAANDIGDTT NRSNEIPSTD VTDKTGREH LEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
-
Background
NTRK2, also known as TrkB, is a high-affinity receptor for BDNF and other neurotrophins such as neurotrophin-4 (NT-4) and neurotrophin-3 (NT-3). It plays a crucial role in the development, function, and plasticity of the nervous system. Dysregulation of NTRK2 signaling is associated with various neurological disorders, including neurodegenerative diseases, psychiatric disorders, and cancers. NTRK2 has been developed to facilitate research into its biological functions and potential therapeutic applications. This paper provides a comprehensive overview of the scientific research on recombinant human NTRK2, focusing on its biological functionality, detailed description, and physical properties.
NTRK2 is critical for synaptic plasticity, which underlies learning and memory. Research with rhNTRK2 has demonstrated that BDNF-NTRK2 signaling enhances synaptic strength and facilitates long-term potentiation (LTP) in hippocampal neuron.
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 :
SCGB1A1 Human, HisDescription:
Uteroglobin Human Recombinant, His Tag
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Product # :
CYT-752Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Uteroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 9.2kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
-
Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1A1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHASEICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.
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 :
LCN2 RatDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Rat Recombinant
Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.
Product # :
ENZ-920Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LCN2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (21-198 a.a) and having a molecular mass of 22.9kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core. They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.
-
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.
-
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 MGSQDSTQNL IPAPPLISVP LQPGFWTERF QGRWFVVGLA ANAVQKERQS RFTMYSTIYE LQEDNSYNVT SILVRGQGCR YWIRTFVPSS RPGQFTLGNI HSYPQIQSYD VQVADTDYDQ FAMVFFQKTS ENKQYFKVTL YGRTKGLSDE LKERFVSFAK SLGLKDNNIV FSVPTDQCID N.
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 :
CD105 Human, Sf9Description:
Endoglin Human Recombinant, Sf9
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-389Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.More Info
-
Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities. -
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
-
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 90kDa.
What is the source or expression system of CD105 Protein?
Sf9 Insect Cells.
What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.
What is the amino acid sequence of CD105 Protein?
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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 :
ACVRL1 HumanDescription:
Activin A Receptor Type II-Like 1 Human Recombinant
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
Product # :
CYT-920Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
-
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
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
-
Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.
What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.
What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 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 :
SCGB1D1 HumanDescription:
Secretoglobin Family 1D, Member 1 Human Recombinant
Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.
Product # :
PRO-1602Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SCGB1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-90) containing 79 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 8.8kDa (calculated).
Source
Escherichia Coli.
Formulation
SCGB1D1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).
-
Synonyms
Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1D1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHAS VVCQALGSEI TGFLLAGKPV FKFQLAKFKA PLEAVAAKME VKKCVDTMAY EKRVLITKTL GKIAEKCDR.
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 :
NUBP2 HumanDescription:
Nucleotide Binding Protein 2 Human Recombinant
Nucleotide Binding Protein 2, Nucleotide Binding Protein 2 (MinD Homolog, E. Coli), NBP 2,CFD1, C447E6.1 (Nucleotide Binding Protein 1 (E.Coli MinD Like) ), Homolog Of Yeast Cytosolic Fe-S Cluster Deficient 1, Nucleotide Binding Protein 2 (E.Coli MinD Like), Cytosolic Fe-S Cluster Assembly Factor NUBP2, Nucleotide-Binding Protein 2, NUBP1, NUBP2.
Product # :
PRO-2133Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NUBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-271 a.a) and having a molecular mass of 31.2kDa.NUBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUBP2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nucleotide Binding Protein 2, also known as NUBP2 is an adenosine triphosphate (ATP) as well as metal-binding protein which is essential for the assembly of cyotosolic iron-sulfur proteins. NUBP2 performs in a heterotetramer with nucleotide-binding protein 1 (NUBP1). Moreover, alternative splicing results in multiple transcript variants have been found for NUBP2.
-
Synonyms
Nucleotide Binding Protein 2, Nucleotide Binding Protein 2 (MinD Homolog, E. Coli), NBP 2,CFD1, C447E6.1 (Nucleotide Binding Protein 1 (E.Coli MinD Like) ), Homolog Of Yeast Cytosolic Fe-S Cluster Deficient 1, Nucleotide Binding Protein 2 (E.Coli MinD Like), Cytosolic Fe-S Cluster Assembly Factor NUBP2, Nucleotide-Binding Protein 2, NUBP1, NUBP2.
-
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 MGSMEAAAEP GNLAGVRHII LVLSGKGGVG KSTISTELAL ALRHAGKKVG ILDVDLCGPS IPRMLGAQGR AVHQCDRGWA PVFLDREQSI SLMSVGFLLE KPDEAVVWRG PKKNALIKQF VSDVAWGELD YLVVDTPPGT SDEHMATIEA LRPYQPLGAL VVTTPQAVSV GDVRRELTFC RKTGLRVMGI VENMSGFTCP HCTECTSVFS RGGGEELAQL AGVPFLGSVP LDPALMRTLE EGHDFIQEFP GSPAFAALTS IAQKILDATP ACLP
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 :
Leuprorelin HumanDescription:
Leuprolide Human
Leuprolide, Leuprorelin.
Product # :
HOR-260Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Leuprolide Human Synthetic is a single, non-glycosylated, polypeptide chain containing 9 amino acids and having a molecular mass of 1209 Dalton. The molecular formula is C59H84N16O12.
Formulation
The Leuprorelin was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
-
Introduction
Leuprorelin (INN) or leuprolide acetate (USAN) is a gonadotropin-releasing hormone agonist (GnRH agonist).
By causing constant stimulation of the pituitaryGnRH receptors, it initially causes stimulation (flare), but thereafter decreases pituitary secretion (downregulation) of gonadotropins luteinizing hormone(LH) and follicle-stimulating hormone(FSH).
Like other GnRH agonists, leuprolide may be used in the treatment of hormone-responsive cancers such as prostate canceror breast cancer, estrogen-dependent conditions (such as endometriosisor uterine fibroids), to treat precocious puberty, and to control ovarian stimulation in IVF. -
Synonyms
Leuprolide, Leuprorelin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leoprolide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leuprorelin 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 Leoprolide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
pGlu-His-Trp-Ser-Tyr-D-Leu-Leu-Arg-Pro-NHEt.
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 :
NPPA HumanDescription:
Natriuretic Peptide A Human Recombinant
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Product # :
CYT-1028Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).
Source
Escherichia Coli.
Formulation
NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
-
Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.
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 :
NCS1 HumanDescription:
Neuronal Calcium Sensor 1 Human Recombinant
Frequenin homolog, FLUP, FREQ, Neuronal calcium sensor 1, Frequenin-like protein, Frequenin-like ubiquitous protein, NCS-1, NCS1, DKFZp761L1223.
Product # :
PRO-802Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NCS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (1-190 a.a.) and having a molecular mass of 22.9 kDa. The NCS1 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NCS1 solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
NCS1 is part of the neuronal calcium sensor gene family, which encode calcium-binding proteins expressed primarily in neurons. NCS1 regulates G protein-coupled receptor phosphorylation in a calcium-dependent manner and can substitute for calmodulin. NCS1 is related with secretory granules and modulates synaptic transmission and synaptic plasticity. NCS1 regulates GRK1 and substitutes for calmodulin. NCS1 stimulates PI4KB kinase activity and participates in long-term synaptic plasticity through its interaction with PICK1. NCS1 takes part in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel.
-
Synonyms
Frequenin homolog, FLUP, FREQ, Neuronal calcium sensor 1, Frequenin-like protein, Frequenin-like ubiquitous protein, NCS-1, NCS1, DKFZp761L1223.
-
Physical Appearance
Sterile Filtered clear 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
MGKSNSKLKP EVVEELTRKT YFTEKEVQQW YKGFIKDCPS GQLDAAGFQK IYKQFFPFGD PTKFATFVFN VFDENKDGRI EFSEFIQALS VTSRGTLDEK LRWAFKLYDL DNDGYITRNE MLDIVDAIYQ MVGNTVELPE EENTPEKRVD RIFAMMDKNA DGKLTLQEFQ EGSKADPSIV QALSLYDGLV LEHHHHHH.
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 :
VEGF (121 a.a.) HumanDescription:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-343Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.
More Info
-
Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HistrelinDescription:
Histrelin
Product # :
HOR-244Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Histrelin has a molecular formula of C66H86N18O12, a.a. sequence of Pyr-His-Trp-Ser-Tyr-D-His(Bzl)-Leu-Arg-Pro-NHEt and having a Mw of 1323.32 Dalton.
Formulation
The Histrelin peptide was lyophilized with no additives.
Purity
Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Histrelin is a hormone similar to one normally released from the hypothalamus gland in the brain. Histrelin works by decreasing the amount of estrogen and testosterone in the blood. Suppressing estrogen can cause thinning of the bones or slowing of their growth. Histrelin acetate is a potent LHRH agonist which stimulates LH and FSH release and inhibits the actions of sex steroids on the male and female reproductive tracts. After a transient increase, continuous administration results in down regulation of LH and FSH levels followed by a suppression of ovarian and testicular steroid biosynthesis. Histrelin potency in vivo and in vitro is similar to that of the D-Trp6-containing analog. Especially because of its high water solubility and greater lipophilic character, it appears promising for clinical application.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Histrelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Histrelin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Histrelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PSMD10 AntibodyDescription:
Gankyrin, Mouse Anti Human
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
Product # :
ANT-609Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.
-
Synonyms
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human PSMD10 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PSMD10 protein 1-226 amino acids purified from E.coli.
-
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
-
Clone
PAT1F4AT.
-
Applications
PSMD10 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
PSMD10 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Thymosin beta 4Description:
Thymosin β4
Thymosin beta-4. TB500, TB-500
Product # :
HOR-275Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
-
Introduction
Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.
-
Synonyms
Thymosin beta-4. TB500, TB-500
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
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 :
NTRK1 RatDescription:
Neurotrophic Receptor Tyrosine Kinase 1 Rat Recombinant
TRKA, TRK-A, NTRK-1.
Product # :
PKA-133Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
NTRK1 Rat Recombinant produced in HEK is a single, non-glycosylated polypeptide chain containing 623 amino acids (35-418 a.a) and having a molecular mass of 69 kDa. NTRK1 is fused to a 239 amino acid human IgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTRK1 protein solution (1mg/ml) in Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit NGF-induced proliferation assay using TF1 human erythroleukemic cells in the presence of 0.5ng/ml of rat NGF. The ED50 range ≤ 5 ng/ml.
More Info
-
Introduction
NTRK1 plays a role in the development and survival of nerve cells (neurons), specifically those that transmit dataregarding senses such as touch, pain and temperatureie. sensory neurons. NTRK1 protein is located on surface cells, mainly such as sensory neurons. NTRK1 acts as a kinase enzyme that alters the activity of different proteins by adding anoxygen cluster and phosphorus atoms at precise positions ie. phosphorylation. NTRK1 activated by nerve growth factor beta which binds to it and signals the NTRK1 protein to phosphorylate itself. Post autophosphorylation, the activated NTRK1 protein phosphorylates other proteins which is required for cell growth and survival.
-
Synonyms
TRKA, TRK-A, NTRK-1.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
NTRK1 although stable at 4°C for 1 week, should be stored 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.
-
Amino Acid Sequence
SCRETCCPVG PSGLRCTRAG TLNTLRGLRG AGNLTELYVE NQRDLQRLEF EDLQGLGELR SLTIVKSGLR FVAPDAFHFT PRLSHLNLSS NALESLSWKT VQGLSLQDLT LSGNPLHCSC ALLWLQRWEQ EDLCGVYTQK LQGSGSGDQF LPLGHNNSCG VPSVKIQMPN DSVEVGDDVF LQCQVEGQAL QQADWILTEL EGTATMKKSG DLPSLGLTLV NVTSDLNKKN VTCWAENDVG RAEVSVQVSV SFPASVHLGK AVEQHHWCIP FSVDGQPAPS LRWFFNGSVL NETSFIFTQF LESALTNETM RHGCLRLNQP THVNNGNYTL LAANPYGQAA ASIMAAFMDN PFEFNPEDPI PVSFSPVDTN STSRDPVEKK DETP LEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH
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 :
BuserelinDescription:
Buserelin
Product # :
HOR-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.
Formulation
The Buserelin peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Buserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Buserelin 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 Buserelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
REG4 HumanDescription:
Regenerating Islet-Derived 4 Human Recombinant
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
Product # :
PRO-424Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add deionized water to a working concentration approximately 0.5 mg/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.
-
Amino Acid Sequence
MKHHHHHHAS HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.
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 :
Insulin HumanDescription:
Insulin Human Recombinant
Product # :
CYT-270Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Insulin Human Recombinant produced in E.Coli is a two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC analysis.
Biological Activity
The Biological Activity was determined to be 28 units/mg.More Info
-
Introduction
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Insulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Insulin 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 Insulin in sterile 0.005N HCl not more than 1 mg/ml.
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 :
PPARG Human (1-477)Description:
Peroxisome Proliferator Activated Receptor Gamma Human Recombinant, (1-477 a.a)
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
Product # :
PKA-334Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- More Info
Description
PPARG Human Recombinant encoding amino acids 1-477 expressed in E.coli, is fused to a GST tag and it is antibody reactive.The PPARG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPARG at 0.1mg/ml in 50mM Tris-HCl and 10mM L-glutathione (reduced).
More Info
-
Introduction
Peroxisome proliferators are non-genotoxic carcinogens which are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed peroxisome proliferators activated receptors (PPARs). Nuclear hormone receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Studies indicate that PPARs are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY-14,643, as well as by some fatty acids.
-
Synonyms
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Avoid multiple freeze-thaw cycles.
-
Applications
ELISA.
Inhibition Assays.
Western Blotting.
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 :
sRANKL HumanDescription:
RANK Ligand Soluble Human Recombinant
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.
Product # :
CYT-334Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- HPLC, SDS-PAGE
Description
sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Sodium phosphate, pH-7.5.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x104 units/mg.
HPLC, SDS-PAGE
More Info
-
Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
-
Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL 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 sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.
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.