Search: 44 results found for "N-Myc Downstream Regulated"

Description:

26S proteasome non-ATPase regulatory subunit 11 clone PAT2C7AT Mouse Anti Human

26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit RPN6, 26S proteasome regulatory subunit p44.5, PSMD11, S9, Rpn6, p44.5, MGC3844.

Product # :

ANT-675

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Formulation

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

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Introduction
The 26S proteasome is a multicatalytic proteinase complex with a well ordered structure composed of two complexes- a 20S core and a 19S regulator. PSMD11 is a non-ATPase subunit of the 19S regulator. The 20S core is composed of four rings of 28 non-identical subunits; two rings are composed of 7 alpha subunits and two rings are composed of 7 beta subunits. The 19S regulator is composed of a base that contains six ATPase subunits and two non-ATPase subunits, and a lid that contains up to ten non-ATPase subunits. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An indispensable function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.
Synonyms
26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit RPN6, 26S proteasome regulatory subunit p44.5, PSMD11, S9, Rpn6, p44.5, MGC3844.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human PSMD11 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PSMD11 PAT2C7AT amino acids 1-422 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and ? light chain.
Clone
PAT2C7AT.
Applications
PSMD11 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
PSMD11 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.

Description:

Tyrosine Kinase ErbB-3 Mouse Recombinant

Receptor tyrosine-protein kinase erbB-3, Glial growth factor receptor, Proto-oncogene-like protein c-ErbB-3.

Product # :

PKA-085

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Description

ErbB3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 630 amino acids (20-641.a.) and having a molecular mass of 69.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ErbB3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ErbB3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.
Synonyms
Receptor tyrosine-protein kinase erbB-3, Glial growth factor receptor, Proto-oncogene-like protein c-ErbB-3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SEMGNSQAVC PGTLNGLSVT GDADNQYQTL YKLYEKCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSVLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRFTQL TEILLGGVYI EKNDKLCHMD TIDWRDIVRV PDAEIVVKNN GGNCPPCHEV CKGRCWGPGP EDCQILTKTI CAPQCNGRCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PAPLVYNKLT FQLEPNPHIK YQYGGVCVAS CPHNFVVDQT FCVRACPADK MEVDKNGLKM CEPCRGLCPK ACEGTGSGSR YQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRVYISAN QQLCYHHSLN WTRLLRGPAE ERLDIKYNRP LGECVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSREGVC VTHCNVLQGE PREFVHEAHC FSCHPECQPM EGTSTCNGSG SDACARCAHF RDGPHCVNSC PHGILGAKGP IYKYPDAQNE CRPCHENCTQ GCKGPELQDC LGQAEVLMSK PHLEHHHHHH.

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.

Description:

Cellular Retinoic Acid binding Protein 1 Human Recombinant

Cellular retinoic acid-binding protein 1, Cellular retinoic acid-binding protein I, CRABP-I, CRABP1, RBP5, CRABP, CRABPI.

Product # :

PRO-710

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Description

CRABP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15.5kDa. The CRABP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRABP1 (1mg/ml) protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CRABP1 is a member of special carrier proteins for members of the vitamin A family. It is believed that CRABP1 has an essential role in retinoic acid-mediated differentiation and proliferation processes. Though, CRABP1 is structurally similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. CRABP1 is constitutively expressed and is thought to have different functions in the cell than the related CRABP2. CRABP1 forms a beta-barrel structure which accommodates hydrophobic ligands in its interior.
Loss of CRABP1 function as a result of hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma. Furthermore, frequent methylation-associated silencing of CRABP1 is linked to esophageal squamous-cell carcinoma.
Synonyms
Cellular retinoic acid-binding protein 1, Cellular retinoic acid-binding protein I, CRABP-I, CRABP1, RBP5, CRABP, CRABPI.
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
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR TTEINFKVGE GFEEETVDGR KCRSLATWEN ENKIHCTQTL LEGDGPKTYW TRELANDELI LTFGADDVVC TRIYVRE.

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.

Description:

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-334

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HPLC, SDS-PAGE
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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 2.1x10⁴units/mg.

HPLC, SDS-PAGE

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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.

Description:

Fibroblast Growth Factor-23 Human Recombinant

Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

Product # :

CYT-020

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Description

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
Background
Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.
Mechanism
Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.
Interactions
Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.
Function
Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.
Structure
FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.
What is the molecular weight/Mw of FGF23 HUMAN Protein?
FGF23 HUMAN Protein has a total Mw of 22.5kDa.

What is the source or expression system of FGF23 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF23 HUMAN Protein?
FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF23 HUMAN Protein?
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

What is the amino acid sequence of FGF23 HUMAN Protein?
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

What applications can FGF23 HUMAN Protein be used in?
FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF23 HUMAN Protein?
The endotoxin level is minimal, FGF23 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.

Description:

Bcl-2 homologous antagonist/killer, Mouse Anti Human

Bcl-2 homologous antagonist/killer, Apoptosis regulator BAK, Bcl-2-like protein 7, Bcl2-L-7, BAK1, BAK, BCL2L7, CDN1, MGC3887, BAK-LIKE, MGC117255.

Product # :

ANT-015

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
BAK1 is a member of the BCL2 protein family. The BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators which are involved in a wide variety of cellular activities. The BAK1 gene encodes a receptor-like kinase (RLK) with a putative extracellular domain, a single transmembrane domain, an intracellular-juxtamembrane domain, and a kinase domain. BAK1 localizes to mitochondria, and functions to induce apoptosis. BAK1 interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, leading to a loss in membrane potential and the release of cytochrome c. Furthermore, BAK1 interacts with the tumor suppressor P53 after exposure to cell stress. BAK1 expression is linked to the progression of Prostate cancer.
Synonyms
Bcl-2 homologous antagonist/killer, Apoptosis regulator BAK, Bcl-2-like protein 7, Bcl2-L-7, BAK1, BAK, BCL2L7, CDN1, MGC3887, BAK-LIKE, MGC117255.
Immunogen
Anti-human BAK1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human BAK1 amino acids 29-187 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT38E2AT.
Applications
BAK1 antibody has been tested by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:250 ~ 500.
Recommended starting dilution is 1:250.
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
BAK1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Chloride Channel, Nucleotide-Sensitive, 1A Human Recombinant

CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.

Product # :

PRO-1277

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Description

CLNS1A Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.8kDa (molecular size on SDS-PAGE will appear higher).CLNS1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CLNS1A solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Methylosome subunit pICln (CLNS1A), is a member of the pICln (TC 1.A.47) family. CLNS1A takes part in multiple regulatory pathways. CLNS1A interaction with Sm proteins, inhibits their compilation on U RNA and interferes with snRNP biogenesis. CLNS1A inhibits the binding of survival motor neuron protein (SMN) to Sm proteins. Methylosome subunit pICln is related with the plasma membrane where it functions as a chloride present regulator.
Synonyms
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
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 MGSHMSFLKS FPPPGPAEGL LRQQPDTEAV LNGKGLGTGT LYIAESRLSW LDGSGLGFSL EYPTISLHAL SRDRSDCLGE HLYVMVNAKF EEESKEPVAD EEEEDSDDDV EPITEFRFVP SDKSALEAMF TAMCECQALH PDPEDEDSDD YDGEEYDVEA HEQGQGDIPT FYTYEEGLSH LTAEGQATLE RLEGMLSQSV SSQYNMAGVR TEDSIRDYED GMEVDTTPTV AGQFEDADVD H.

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Description:

Minichromosome Maintenance Complex Component 7 Human Recombinant

Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.

Product # :

PRO-1847

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Description

MCM7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 48.6 kDa. MCM7 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The MCM7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.
Synonyms
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVVATYT CDQCGAETYQ PIQSPTFMPL IMCPSQECQT NRSGGRLYLQ TRGSRFIKFQ EMKMQEHSDQ VPVGNIPRSI TVLVEGENTR IAQPGDHVSV TGIFLPILRT GFRQVVQGLL SETYLEAHRI VKMNKSEDDE SGAGELTREE LRQIAEEDFY EKLAASIAPE IYGHEDVKKA LLLLLVGGVD QSPRGMKIRG NINICLMGDP GVAKSQLLSY IDRLAPRSQY TTGRGSSGVG LTAAVLRDSV SGELTLEGGA LVLADQGVCC IDEFDKMAEA DRTAIHEVME QQTISIAKAG ILTTLNARCS ILAAANPAYG RYNPRRSLEQ NIQLPAALLS RFDLLWLIQD RPDRDNDLRL AQHITYVHQH SRQPPSQFEP LDMKLMRRYI AMCREKQPMV PESLADYITA AYVEMRR

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Description:

Tumor Necrosis Factor-Alpha Rat Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-393

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Description

Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-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.
Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.

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.

Description:

Delta Sleep Inducing Peptide

Product # :

HOR-030

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Description

DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

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 DSIP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DSIP 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 DSIP 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-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
Background
Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.
DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.
In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.
While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.

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.

Description:

Cyclin-Dependent Kinase Inhibitor 2A Human Recombinant, TAT

Cyclin-dependent kinase 4 inhibitor A, CDK4I, p16-INK4, p16-INK4a, p16INK4A, CDKN-2A, CDKN2, Multiple tumor suppressor 1, MTS1, CMM2, MLM, TP16, p16(INK4), p19.

Product # :

PKA-337

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

p16-INK4a Human Recombinant is a single, non-glycosylated, polypeptide chain produced in E.coli, containing a total of 168 amino acids, which includes the 156 residues of full-length p16-INK4a and a 13-residue C-terminal TAT peptide (GGYGRKKRRQRRR), having a total Mw of 18kDa. p16-INK4a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

More Info

Introduction
Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.
Synonyms
Cyclin-dependent kinase 4 inhibitor A, CDK4I, p16-INK4, p16-INK4a, p16INK4A, CDKN-2A, CDKN2, Multiple tumor suppressor 1, MTS1, CMM2, MLM, TP16, p16(INK4), p19.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized p16-INK4a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution p16-INK4a 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 p16-INK4a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EPAAGSSMEP SADWLATAAA RGRVEEVRAL LEAGALPNAP NSYGRRPIQV MMMGSARVAE LLLLHGAEPN CADPATLTRP VHDAAREGFL DTLVVLHRAG ARLDVRDAWG RLPVDLAEEL GHRDVARYLR AAAGGTRGSN HARIDAAEGP SDIPDGGYGR KKRRQRRR.

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.

Description:

Leptin Chicken Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-505

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Description

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

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.

Description:

Interleukin-1 Receptor Antagonist Rat Recombinant, His Tag

Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.

Product # :

CYT-899

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (27-178a.a.) and having a molecular mass of 19.8kDa.IL 1RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 1RA protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.
Background
What is the molecular weight/Mw of IL1RA RAT, HIS Protein?
IL1RA RAT, HIS Protein has a total Mw of 19.8kDa.

What is the source or expression system of IL1RA RAT, HIS Protein?
Escherichia Coli.

What is the Purity of IL1RA RAT, HIS Protein?
IL1RA RAT, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RA RAT, HIS Protein?
The biological functionality of IL1RA RAT, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1RA RAT, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.

What applications can IL1RA RAT, HIS Protein be used in?
IL1RA RAT, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RA RAT, HIS Protein?
The endotoxin level is minimal, IL1RA RAT, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RA RAT, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL1RA RAT, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Cyclin-Dependent Kinase 1 Human Recombinant

Cyclin-Dependent Kinase 1, CDC2, Cell Division Cycle 2, G1 To S And G2 To M, Cell Division Control Protein 2 Homolog, Cell Division Protein Kinase 1, P34 Protein Kinase, P34CDC2, CDC28A, Cell Cycle Controller CDC2, EC 2.7.11.22, EC 2.7.11.23, CDKN1, Cyclin-dependent kinase 1, CDK1.

Product # :

PKA-076

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Shipped with Ice Packs

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Description

CDK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 36.2kDa. CDK1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDK1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Cyclin-dependent kinase 1 (CDK1) plays a significant part in the control of the eukaryotic cell cycle through modulating the centrosome cycle in addition to mitotic onset; CDK1 promotes G2-M transition and regulates G1 progress and G1-S transition using association with multiple interphase cyclins. CDK1 is essential in higher cells for the entry into S-phase and mitosis.
Synonyms
Cyclin-Dependent Kinase 1, CDC2, Cell Division Cycle 2, G1 To S And G2 To M, Cell Division Control Protein 2 Homolog, Cell Division Protein Kinase 1, P34 Protein Kinase, P34CDC2, CDC28A, Cell Cycle Controller CDC2, EC 2.7.11.22, EC 2.7.11.23, CDKN1, Cyclin-dependent kinase 1, CDK1.
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 MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT FPKWKPGSLA SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM.

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.

Description:

Human Glucagon Like Peptide-1

GLP1, Glucagon Like Peptide-1, Incretin hormone.

Product # :

HOR-284

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Quantity :

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Shipped at Room temp

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Description

Glucagon Like Peptide-1 is a single, non-glycosylated, polypeptide chain containing 30 amino acids and having a molecular mass of 3297.7 Dalton.The GLP-1 is purified by proprietary chromatographic techniques.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 96.0% as determined by RP-HPLC.

More Info

Introduction
Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.
Synonyms
GLP1, Glucagon Like Peptide-1, Incretin hormone.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-1 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 Glucagon Like Peptide-1 in sterile H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-NH2.
Background
What is the molecular weight/Mw of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
GLUCAGON-LIKE PEPTIDE1 HUMAN Protein has a total Mw of 3.297kDa.

What is the Purity of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
GLUCAGON-LIKE PEPTIDE1 HUMAN Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
The biological functionality of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-NH2.

What applications can GLUCAGON-LIKE PEPTIDE1 HUMAN Protein be used in?
GLUCAGON-LIKE PEPTIDE1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GLUCAGON-LIKE PEPTIDE1 HUMAN Protein?
The endotoxin level is minimal, GLUCAGON-LIKE PEPTIDE1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies GLUCAGON-LIKE PEPTIDE1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GLUCAGON-LIKE PEPTIDE1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Transforming Growth Factor Beta 2 Human Recombinant

Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

Product # :

CYT-441

Price :

Quantity :

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Shipped at Room temp

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Description

TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

More Info

Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human 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 TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

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.

Description:

Goserelin

Product # :

HOR-256

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Quantity :

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Description

Goserelin contains 10 amino acids Glu1-His2-Trp3-Ser4-Tyr5-D-Ser(tBu)6-Leu7-Arg8-Pro9-AzGly10-NH2 and having a molecular weight of 1269.43 Dalton.

Formulation

The protein (1 mg/ml) 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
Goserelin is a hormone similar to the one normally released from the hypothalamus gland in the brain (GnRH super-agonist). It is used to treat for prostate and breast cancer.
Goserelin decreases the amount of estrogen and testosterone by this treating endometriosis and cancer of the breast, and can help thin the uterus lining before surgery. Goserelin prevents the growth of tissue associated with endometriosis.
Reducing the amount of testosterone is one way of treating prostate cancer.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Goserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Goserelin 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 Goserelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of GOSERELIN Protein?
GOSERELIN Protein has a total Mw of 1.269kDa.

What is the Purity of GOSERELIN Protein?
GOSERELIN Protein is >98% pure as determined by SDS-PAGE.

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

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

What is the endotoxin level for GOSERELIN Protein?
The endotoxin level is minimal, GOSERELIN Protein was purified using conventional chromatography techniques.

Who supplies GOSERELIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GOSERELIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Pramlintide

Product # :

HOR-300

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Pramlintide Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 3949.4 Dalton and a Molecular formula of C171H267N51O53S2.

Formulation

The protein 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
Pramlintide acetate is a hormone that is released into the bloodstream, in a similar pattern as insulin. Pramlintide aids in the absorption of glucose by slowing gastric emptying, promoting satiety, and inhibiting inappropriate secretion of glucagon, a catabolic hormone that opposes the effects of insulin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pramlintide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pramlintide 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 Pramlintide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. The Pramlintide is also soluble in 1% Acetic Acid.
Amino Acid Sequence
KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY-NH2.
Background
What is the molecular weight/Mw of PRAMLINTIDE Protein?
PRAMLINTIDE Protein has a total Mw of 3.949kDa.

What is the Purity of PRAMLINTIDE Protein?
PRAMLINTIDE Protein is >98% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of PRAMLINTIDE Protein?
KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY-NH2.

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

What is the endotoxin level for PRAMLINTIDE Protein?
The endotoxin level is minimal, PRAMLINTIDE Protein was purified using conventional chromatography techniques.

Who supplies PRAMLINTIDE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of PRAMLINTIDE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-1 Receptor Antagonist Human Recombinant

IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

Product # :

CYT-203

Price :

Quantity :

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Shipped at Room temp

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formulation
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Description

IL1ra Human Recombinant produced in E.Coli is a non-glycosylated, N-terminal methionyl form of the human naturally-occurring polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton. The IL1ra is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized protein with no additives.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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 Interleukin-1 ra in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.
Background
What is the molecular weight/Mw of IL 1RA HUMAN Protein?
IL 1RA HUMAN Protein has a total Mw of 17kDa.

What is the source or expression system of IL 1RA HUMAN Protein?
Escherichia Coli.

What is the Purity of IL 1RA HUMAN Protein?
IL 1RA HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 1RA HUMAN Protein?
The ED50 as determined by the dose-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.

What is the amino acid sequence of IL 1RA HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.

What applications can IL 1RA HUMAN Protein be used in?
IL 1RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 1RA HUMAN Protein?
The endotoxin level is minimal, IL 1RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 1RA HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 1RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 ra as a Reference Standard.

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.

Description:

Parathyroid Hormone (1-34) Human Recombinant

Parathyrin, PTH, Parathormone.

Product # :

HOR-247

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

Parathyroid Hormone Human Recombinant (C181H290N55O51S2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 34 amino acids and having a molecular mass of 4117.8 Dalton. The PTH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1 mg/ml) was lyophilized after extensive dialyses against 1.15 mg sodium citrate, sodium chloride 7.31 mg, 0.21 mg citric acid, 0.1117 EDTA-Na2, 0.2 mg Tween 80 and 50 mg Mannitol.

Purity

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

Biological Activity

The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 10,000 Units/mg.

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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures.
Synonyms
Parathyrin, PTH, Parathormone.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH 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 Parathormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-Asn-Leu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-Arg-Val-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe.
Background
What is the molecular weight/Mw of PARATHORMONE HUMAN Protein?
PARATHORMONE HUMAN Protein has a total Mw of 4.117kDa.

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

What is the Purity of PARATHORMONE HUMAN Protein?
PARATHORMONE HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of PARATHORMONE HUMAN Protein?
The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 10,000 Units/mg.

What is the amino acid sequence of PARATHORMONE HUMAN Protein?
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-Asn-Leu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-Arg-Val-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe.

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

What is the endotoxin level for PARATHORMONE HUMAN Protein?
The endotoxin level is minimal, PARATHORMONE HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant PARATHORMONE HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of PARATHORMONE HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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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