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1000 results found for “Calcyphosine”
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Name :
PSPH AntibodyDescription:
Phosphoserine Phosphatase, Mouse Anti Human
Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.
Product # :
ANT-399Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.
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Synonyms
Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.
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Immunogen
Anti-human PSPH mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PSPH amino acids 1-225 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P3G12AT.
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Applications
PSPH antibody has been tested by ELISA and Western blot 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 is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
PSPH 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.
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Name :
G CSF Human, CHODescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, CHO
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-329Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Colony Stimulating Factor Human Recombinant produced in CHO cells is a single, glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18 kDa.G-CSF is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells (CHO).
Formulation
G-CSF was lyophilized from a concentrated (1mg/ml) solution containing 10mM Hydrochloric Acid pH=6.5, 0.4mg tween 20, 100mg mannitol, 160mg L-arginine, 40mg phenylalanine and 4mg methionine.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.07 ng/ml, corresponding to a Specific Activity of 1.27 x 108 IU/mg.More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Granulocyte Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP.
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Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 18kDa.
What is the source or expression system of G CSF Protein?
Chinese Hamster Ovary Cells (CHO).
What is the Purity of G CSF Protein?
G CSF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF Protein?
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.07 ng/ml, corresponding to a Specific Activity of 1.27 x 108 IU/mg.
What is the amino acid sequence of G CSF Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP.
What applications can G CSF Protein be used in?
G CSF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF Protein?
The endotoxin level is minimal, G CSF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
B.Microti p41Description:
Babesia Microti p41 Recombinant
Product # :
PRO-2567Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Babesia Microti p41 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 38kDa. B.Microti p41 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
B.Microti p41 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Babesiosis is a disease caused by apicomplexan parasites of the Babesia genus. The Babesia microti life cycle involves 2 hosts, which include a rodent, mainly the white-footed mouse (Peromyscus leucopus) and a tick in the Ixodes genus. During a blood meal, a Babesia-infected tick introduces sporozoites into the mouse host. Sporozoites pass into the erythrocytes and undergo asexual reproduction (budding). In the blood, some parasites differentiate into male and female gametes, though these cannot be distinguished by light microscopy. The definitive host is the tick. Once ingested by an proper tick, gametes unite and undergo a sporogonic cycle resulting in sporozoites. Transovarial transmission (aka vertical or hereditary transmission) has been detected for "large" Babesia species but not for the "small" Babesia, such as B. microti. Humans enter the cycle when bitten by the infected ticks. Thus during a blood meal, a Babesia-infected tick introduces sporozoites into the human host. Sporozoites then enter erythrocytes and undergo asexual replication (budding). Multiplication of the blood-stage parasites is responsible for the clinical manifestations of the disease. Humans typically are dead-end hosts. However, human-to-human transmission is well acknowledged to occur via contaminated blood transfusions.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
YWHAQ AntibodyDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta, Mouse Anti Human
14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.
Product # :
ANT-387Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.
More Info
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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.
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Synonyms
14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.
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Immunogen
Anti-human YWHAQ mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human YWHAQ amino acids 1-245 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PAT1A1AT.
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Applications
YWHAQ antibody has been tested by ELISA and Western blot 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 is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
YWHAQ 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.
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Name :
LypressinDescription:
Lypressin
Product # :
HOR-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lypressin is a hormone used to prevent or control the frequent urination, increased thirst, and loss of water associated with diabetes insipidus (water diabetes). Its molecular weight is 1056.2 Dalton having an amino acid sequence of Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Lys-Gly-NH2. The Molecular Formula is: C46H65N13O12S2. The CAS Number is: 50-57-7.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Lypressin between 2-8°C, do not freeze. Upon reconstitution Lypressin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lypressin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Lypressin is also soluble in 1% Acetic Acid.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VZV ORF9Description:
Varicella Zoster Virus ORF9 Recombinant
Product # :
VZV-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the VZV ORF9 immunodominant regions, amino acids 6-28, 76-100.
Formulation
25mM Tris-Hcl pH 8.0, 1mM EDTA and 50% glycerol.
Purity
Varicella protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
VZV is closely related to the herpes simplex viruses(HSV), sharing much genomehomology. The known envelope glycoproteins (gB, gC, gE, gH, gI, gK, gL) correspond with those in HSV, however there is no equivalent of HSV gD. VZV virons are spherical and 150-200 nm in diameter. Their lipidenvelope encloses the nucleocapsid of 162 capsomeres arranged in a hexagonalform. Its DNAis a single, linear, double-stranded molecule, 125,000 nt long. The virus is very susceptible to disinfectants, notably sodium hypochlorite. Within the body it can be treated by a number of drugs and therapeutic agents including aciclovir, zoster-immune globulin(ZIG), and vidarabine.
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Stability
Varicella protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Immunoreactive with sera of VZV-infected individuals.
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Purification Method
Varicella was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
YWHAE Human, HisDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein, Epsilon Human Recombinant, His Tag
YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.
Product # :
PKA-095Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
YWHAE Human Recombinant produced in E. coli is a single polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 31.3kDa. YWHAE is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YWHAE solution (1mg/1ml) contains phosphate buffered Saline (pH7.4), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.
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Synonyms
YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Lymphotactin HumanDescription:
Lymphotactin Human Recombinant (XCL1)
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-314Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lymphotactin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10007 Dalton. The Lymphotactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The XCL1 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C motif) ligand (XCL1) is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose geneis found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
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Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Lymphotactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution XCL1 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 avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lymphotactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Ser-Glu-Val-Ser.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SPINK7 HumanDescription:
Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant
Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.
Product # :
PRO-1507Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma
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Synonyms
Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NUP62 HumanDescription:
Nucleopurin 62kDa Human Recombinant
Nuclear pore glycoprotein p62, 62 kDa nucleoporin, Nucleoporin Nup62, NUP62, p62, IBSN, SNDI.
Product # :
PRO-999Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NUP62 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 66 kDa. NUP62 is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
NUP62 is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Nucleopurin 62kDa (NUP62) belongs to the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. Nucleoporins are the principal components of the nuclear pore complex in eukaryotic cells. This complex is a colossal structure which extends across the nuclear envelope, forming an entryway that regulates the stream of macromolecules between the nucleus and the cytoplasm. NUP62 associates with the importin alpha/beta complex that is involved in the import of proteins containing nuclear localization signals. Defects in the NUP62 are the cause of SNDI (infantile striatonigral degeneration), aka infantile bilateral striatal necrosis (IBSN) or familial striatal degeneration.
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Synonyms
Nuclear pore glycoprotein p62, 62 kDa nucleoporin, Nucleoporin Nup62, NUP62, p62, IBSN, SNDI.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera), immunodot analysis with positive/negative samples.
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coating concentration
0.5-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with Polyclonal anti-Nup62 antibodies.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TPO Human, HEKDescription:
Thrombopoietin Human Recombinant, HEK
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
Product # :
CYT-115Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thrombopoietin Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 80-85kDa due to glycosylation.The TPO is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The TPO protein was filtered (0.2µm) and lyophilized from 0.74mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The activity was determined by the dose-dependent stimulation of the proliferation of MO7e cells, the ED50 is 1.15ng/ml.
More Info
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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney that regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.
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Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thrombopoietin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TPO should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Thrombopoietin in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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Amino Acid Sequence
SPAPPACDLRVLSKLLRDSHVLHSRLSQCPEVHPLPTPVLLPAVDFSLG EWKTQMEETKAQDILGAVTLLLEGVMAARGQLGPTCLSSLLGQLSGQV RLLLGALQSLLGTQLPPQGRTTAHKDPNAIFLSFQHLLRGKVRFLMLVGG STLCVRRAPPTTAVPSRTSLVLTLNELPNRTSGLLETNFTASARTTGSGLLK WQQGFRAKIPGLLNQTSRSLDQIPGYLNRIHELLNGTRGLFPGPSRRTLGAP DISSGTSDTGSLPPNLQPGYSPSPTHPPTGQYTLFPLPPTLPTPVVQLHPLLPDPSAPTPT
PTSPLLNTSYTHSQNLSQEG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LGALS7 HumanDescription:
Galectin-7 Human Recombinant
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
Product # :
CYT-016Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Galectin-7 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 136 amino acids and having a molecular mass of 15kDa.The LGALS7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LGALS7 was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris, 150mM NaCl, 1mM EDTA and 5% Trehalose, pH 8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.
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Synonyms
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LGALS7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-7 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Galectin-7 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
YHHFRHRLPLARVRLVEVGGDVQLDSVRIF -
Background
What is the molecular weight/Mw of LGALS7 HUMAN Protein?
LGALS7 HUMAN Protein has a total Mw of 15kDa.
What is the source or expression system of LGALS7 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS7 HUMAN Protein?
LGALS7 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS7 HUMAN Protein?
The biological functionality of LGALS7 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS7 HUMAN Protein?
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
YHHFRHRLPLARVRLVEVGGDVQLDSVRIF
What applications can LGALS7 HUMAN Protein be used in?
LGALS7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS7 HUMAN Protein?
The endotoxin level is minimal, LGALS7 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TXN1, HisDescription:
Thioredoxin Recombinant, His Tag
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
Product # :
PRO-784Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TRX His Tag protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >70 A650/cm/min/mg, detected by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
More Info
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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in
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Synonyms
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MHHHHHHMGS DKIIHLTDDS FDTDVLKADG AILVDFWAEW CGPCKMIAPI LDEIADEYQG KLTVAKLNID QNPGTAPKYG IRGIPTLLLF KNGEVAATKV GALSKGQLKE FLDANLAGS.
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 :
GPC4 HumanDescription:
Glypican-4 Human Recombinant
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
Product # :
PRO-1912Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GPC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (401-529a.a) and having a molecular mass of 18kDa.GPC4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GPC4 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.
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Synonyms
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSSSLP SNVCNDERMA AGNGNEDDCW NGKGKSRYLF AVTGNGLANQ GNNPEVQVDT SKPDILILRQ IMALRVMTSK MKNAYNGNDV DFFDISDESS GEGSGSGCEY QQCPSEFDYN ATDHAGKSAN EKADS
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 :
CNPY1 HumanDescription:
Canopy FGF Signaling Regulator 1 Human Recombinant
Protein canopy homolog 1, CNPY1.
Product # :
PRO-1872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CNPY1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-92 a.a) and having a molecular mass of 13.3kDa. CNPY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNPY1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Canopy FGF Signaling Regulator 1, also known as CNPY1, is expressed in the midbrain-hindbrain (MHB) boundary in zebrafish. CNPY1, which binds FGFR1, also takes part in FGF signaling.
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Synonyms
Protein canopy homolog 1, CNPY1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL.
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
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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
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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.
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Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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 :
CRYAB Human, HisDescription:
Crystallin Alpha B Human Recombinant, His Tag
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-088Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.
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Background
Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.
Structural Insights into CRYAB Human Recombinant:
CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.
Cellular Functions in Proteostasis:
As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.
Implications in Neurodegenerative Disorders:
CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.
CRYAB in Cardiovascular Health:
The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.
Challenges and Future Directions:
While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.
CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.
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 :
NKp46 HumanDescription:
Natural Cytotoxicity Receptor NKp46 Human Recombinant
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
Product # :
PRO-432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NKp46 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (22-255) and having a molecular mass of 26.6kDa. NKp46 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NKp46 (1mg/ml) contains phosphate buffered saline (pH7.4) & 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.
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Synonyms
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MQQQTLPKPF IWAEPHFMVP KEKQVTICCQ GNYGAVEYQL HFEGSLFAVD RPKPPERINKVKFYIPDMNS RMAGQYSCIY RVGELWSEPS NLLDLVVTEM YDTPTLSVHP GPEVISGEEV TFYCRLDTAT SMFLLLKEGR SSHVQRGYGK VQAEFPLGPV TTAHRGTYRX FGSYNNHAWSFPSEPVKLLV TGDIENTSLA PEDPTFSADT WGTYLLTTET GLQKDHALWD HTAQN.
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 :
NPL HumanDescription:
N-acetylneuraminate Pyruvate Lyase Human Recombinant
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
Product # :
ENZ-125Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NPL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.
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Synonyms
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.
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 :
CXCL5 HumanDescription:
Epithelial Neutrophil-Activating Protein 78 Human Recombinant (CXCL5)
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
Product # :
CHM-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.More Info
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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II IFN. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
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Background
What is the molecular weight/Mw of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein has a total Mw of 8.02kDa.
What is the source or expression system of CXCL5 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 HUMAN Protein?
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.
What is the amino acid sequence of CXCL5 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
What applications can CXCL5 HUMAN Protein be used in?
CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 HUMAN Protein?
The endotoxin level is minimal, CXCL5 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TARC MouseDescription:
Thymus and Activation Regulated Chemokine (CCL17) Mouse Recombinant
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
Product # :
CHM-270Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
TARC Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7.9kDa. The TARC Mouse is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CCR4 is typically 2-10 ng/ml.More Info
-
Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
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Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TARC should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TARC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ARATNVGREC CLDYFKGAIP IRKLVSWYKT SVECSRDAIV FLTVQGKLIC ADPKDKHVKK AIRLVKNPRP.
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 :
TPMT HumanDescription:
Thiopurine S-methyltransferase Human Recombinant
TPMT, Thiopurine S-methyltransferase, EC 2.1.1.67, Thiopurine methyltransferase.
Product # :
PKA-255Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TPMT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 28 kDa. Thiopurine S-methyltransferase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris 8.0, 0.2mM PMSF and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
TPMT, thiopurine S-methyltransferase, is a cytosolic enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. TPMT activity exhibits autosomal codominant genetic polymorphism, and patients inheriting TPMT-deficiency are at high risk of potentially fatal hematopoietic toxicity.
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Synonyms
TPMT, Thiopurine S-methyltransferase, EC 2.1.1.67, Thiopurine methyltransferase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDGTRTSLDI EEYSDTEVQK NQVLTLEEWQ DKWVNGKTAF HQEQGHQLLK KHLDTFLKGKSGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIQEFF TEQNLSYSEE PITEIPGTKVFKSSSGNISL YCCSIFDLPR TNIGKFDMIW DRGALVAINP GDRKCYADTM FSLLGKKFQY LLCVLSYDPT KHPGPPFYVP HAEIERLFGK ICNIRRLEKV DAFEERHKSW GIDCLFEKLYLLTEK.
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 :
CDC123 HumanDescription:
Cell Division Cycle 123 Human Recombinant
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
Product # :
PRO-1463Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.
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Synonyms
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD
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 :
CDC42 HumanDescription:
Cell Division Cycle 42 Human Recombinant
Cell division control protein 42 homolog, G25K GTP-binding protein, CDC42, G25K, CDC42Hs.
Product # :
PRO-727Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDC42 Human Recombinant fused with a 15 amino acid T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids (1-188 a.a.) and having a molecular mass of 22.4kDa.The CDC42 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDC42 solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 10% glycerol and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CDC42 (Cell division cycle 42 isoform 1) is a small GTPase of the Rho-subfamily that regulates signaling pathways which control various cellular functions including cell morphology, migration, endocytosis and cell cycle progression. CDC42 is a plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In the active state, CDC42 binds to a variety of effector proteins to regulate cellular responses. CDC42 is involved in epithelial cell polarization processes. CDC42 causes the formation of thin, actin-rich surface projections called filopodia. Also, CDC42 regulates actin polymerization through its direct binding to N-WASP (Neural Wiskott-Aldrich syndrome protein), which subsequently activates Arp2/3 complex.
Loss of CDC42 function raises endocytotic uptake of apical proteins, as well as apical polarity factors such as Crumbs. The product of oncogene Dbl was described to specifically catalyze the dissociation of GDP from CDC42 protein. -
Synonyms
Cell division control protein 42 homolog, G25K GTP-binding protein, CDC42, G25K, CDC42Hs.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MASMTGGQQM GRGSHMQTIK CVVVGDGAVG KTCLLISYTT NKFPSEYVPT VFDNYAVTVM IGGEPYTLGL FDTAGQEDYD RLRPLSYPQT DVFLVCFSVV SPSSFENVKE KWVPEITHHC PKTPFLLVGT QIDLRDDPST IEKLAKNKQK PITPETAEKL ARDLKAVKYV ECSALTQKGL KNVFDEAILA ALEPPEPKKS RRC.
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.